Functional and Structural Characterization of OXA-935, a Novel OXA-10-Family β-Lactamase from Pseudomonas aeruginosa

Nathan B. Pincus; Monica Rosas-Lemus; Samuel W.M. Gatesy; Hanna K. Bertucci; Joseph S Brunzelle; George Minasov; Ludmilla A. Shuvalova; Marine Lebrun-Corbin; Karla J.F. Satchell; Egon A. Ozer; Alan R Hauser; Kelly E.R. Bachta

doi:10.1128/aac.00985-22

Functional and Structural Characterization of OXA-935, a Novel OXA-10-Family β-Lactamase from Pseudomonas aeruginosa

Nathan B. Pincus, Monica Rosas-Lemus, Samuel W.M. Gatesy, Hanna K. Bertucci, Joseph S Brunzelle, George Minasov, Ludmilla A. Shuvalova, Marine Lebrun-Corbin, Karla J.F. Satchell, Egon A. Ozer, Alan R Hauser, Kelly E.R. Bachta^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

Resistance to antipseudomonal penicillins and cephalosporins is often driven by the overproduction of the intrinsic b-lactamase AmpC. However, OXA-10-family b-lactamases are a rich source of resistance in Pseudomonas aeruginosa. OXA b-lactamases have a propensity for mutation that leads to extended spectrum cephalosporinase and carbapenemase activity. In this study, we identified isolates from a subclade of the multidrug-resistant (MDR) high risk P. aeruginosa clonal complex CC446 with a resistance to ceftazidime. A genomic analysis revealed that these isolates harbored a plasmid containing a novel allele of bla_OXA-10, named bla_OXA-935, which was predicted to produce an OXA-10 variant with two amino acid substitutions: an aspartic acid instead of a glycine at position 157 and a serine instead of a phenylalanine at position 153. The G157D mutation, present in OXA-14, is associated with the resistance of P. aeruginosa to ceftazidime. Compared to OXA-14, OXA-935 showed increased catalytic efficiency for ceftazidime. The deletion of bla_OXA-935 restored the sensitivity to ceftazidime, and susceptibility profiling of P. aeruginosa laboratory strains expressing bla_OXA-935 revealed that OXA-935 conferred ceftazidime resistance. To better understand the impacts of the variant amino acids, we determined the crystal structures of OXA-14 and OXA-935. Compared to OXA-14, the F153S mutation in OXA-935 conferred increased flexibility in the omega (X) loop. Amino acid changes that confer extended spectrum cephalosporinase activity to OXA-10-family b-lactamases are concerning, given the rising reliance on novel b-lactam/b-lactamase inhibitor combinations, such as ceftolozane-tazobactam and ceftazidime-avibactam, to treat MDR P. aeruginosa infections.

Original language	English (US)
Journal	Antimicrobial agents and chemotherapy
Volume	66
Issue number	10
DOIs	https://doi.org/10.1128/aac.00985-22
State	Published - Oct 2022

Funding

This work was supported by grants from the National Institutes of Health (NIH)/National Institute of Allergy and Infectious Diseases (NIAID) (R01 AI118257, R01 AI053674, U19 AI135964, K24 104831, and R21 AI129167 awarded to A.R.H.), the NIH/National Institute of General Medical Sciences (NIGMS) (T32 GM008061 and T32 GM008152 awarded to N.B.P.), an American Cancer Society (ACS) Postdoctoral Fellowship (number 130602-PF-17-107-01-MPC, awarded to K.E.R.B.), and an ACS Clinician Scientist Development Grant (number 134251-CSDG-20-053-01-MPC, awarded to K.E.R.B.). This project has been funded in whole or in part with federal funds from the NIAID under Contract No. HHSN27201700060C and Grant No. U01AI124316 and R01 GM05789 as well as from the National Institute of Medical Sciences (Grant GM118187), both from the NIH, Department of Health and Human Services. This work used the resources of the Advanced Photon Source, a U.S. Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory under Contract No. DE-AC02-06CH11357. Use of the LS-CAT Sector 21 was supported by the Michigan Economic Development Corporation and the Michigan Technology Tri-Corridor (Grant 085P1000817). This work was also supported by the Northwestern University NUSeq Core Facility, Structural Biology Facility, and High Throughput Analysis Laboratory, which are supported in part by the NCI CCSG P30 CA060553 award to the Robert H. Lurie Comprehensive Cancer Center. This work was also supported in part through the computational resources and staff contributions provided by the Genomics Compute Cluster, which is jointly supported by the Feinberg School of Medicine, the Center for Genetic Medicine, and Feinberg's Department of Biochemistry and Molecular Genetics, Office of the Provost, Office for Research, and Northwestern Information Technology. The Genomics Compute Cluster is part of Quest, Northwestern University's high-performance computing facility, and serves the purpose of advancing research in genomics. The funders had no role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript. We thank members of the Center for Structural Genomics of Infectious Diseases (CSGID) and the Hauser, Ozer, and Kociolek laboratories for their valuable comments during numerous discussions of this work. This work was supported by grants from the National Institutes of Health (NIH)/National Institute of Allergy and Infectious Diseases (NIAID) (R01 AI118257, R01 AI053674, U19 AI135964, K24 104831, and R21 AI129167 awarded to A.R.H.), the NIH/National Institute of General Medical Sciences (NIGMS) (T32 GM008061 and T32 GM008152 awarded to N.B.P.), an American Cancer Society (ACS) Postdoctoral Fellowship (number 130602-PF-17-107-01- MPC, awarded to K.E.R.B.), and an ACS Clinician Scientist Development Grant (number 134251-CSDG-20-053-01-MPC, awarded to K.E.R.B.). This project has been funded in whole or in part with federal funds from the NIAID under Contract No. HHSN27201700060C and Grant No. U01AI124316 and R01 GM05789 as well as from the National Institute of Medical Sciences (Grant GM118187), both from the NIH, Department of Health and Human Services. This work used the resources of the Advanced Photon Source, a U.S. Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory under Contract No. DE-AC02-06CH11357. Use of the LS-CAT Sector 21 was supported by the Michigan Economic Development Corporation and the Michigan Technology Tri-Corridor (Grant 085P1000817). This work was also supported by the Northwestern University NUSeq Core Facility, Structural Biology Facility, and High Throughput Analysis Laboratory, which are supported in part by the NCI CCSG P30 CA060553 award to the Robert H. Lurie Comprehensive Cancer Center. This work was also supported in part through the computational resources and staff contributions provided by the Genomics Compute Cluster, which is jointly supported by the Feinberg School of Medicine, the Center for Genetic Medicine, and Feinberg\u2019s Department of Biochemistry and Molecular Genetics, Office of the Provost, Office for Research, and Northwestern Information Technology. The Genomics Compute Cluster is part of Quest, Northwestern University\u2019s high-performance computing facility, and serves the purpose of advancing research in genomics. The funders had no role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript. We thank members of the Center for Structural Genomics of Infectious Diseases (CSGID) and the Hauser, Ozer, and Kociolek laboratories for their valuable comments during numerous discussions of this work.

Keywords

OXA-b-lactamase
Pseudomonas aeruginosa
antimicrobial resistance
ceftazidime
crystal structure

ASJC Scopus subject areas

Pharmacology
Pharmacology (medical)
Infectious Diseases

Access to Document

10.1128/aac.00985-22

Cite this

Pincus, N. B., Rosas-Lemus, M., Gatesy, S. W. M., Bertucci, H. K., Brunzelle, J. S., Minasov, G., Shuvalova, L. A., Lebrun-Corbin, M., Satchell, K. J. F., Ozer, E. A., Hauser, A. R., & Bachta, K. E. R. (2022). Functional and Structural Characterization of OXA-935, a Novel OXA-10-Family β-Lactamase from Pseudomonas aeruginosa. Antimicrobial agents and chemotherapy, 66(10). https://doi.org/10.1128/aac.00985-22

@article{15c306f7f701496ea63b14923a0aa838,

title = "Functional and Structural Characterization of OXA-935, a Novel OXA-10-Family β-Lactamase from Pseudomonas aeruginosa",

abstract = "Resistance to antipseudomonal penicillins and cephalosporins is often driven by the overproduction of the intrinsic b-lactamase AmpC. However, OXA-10-family b-lactamases are a rich source of resistance in Pseudomonas aeruginosa. OXA b-lactamases have a propensity for mutation that leads to extended spectrum cephalosporinase and carbapenemase activity. In this study, we identified isolates from a subclade of the multidrug-resistant (MDR) high risk P. aeruginosa clonal complex CC446 with a resistance to ceftazidime. A genomic analysis revealed that these isolates harbored a plasmid containing a novel allele of blaOXA-10, named blaOXA-935, which was predicted to produce an OXA-10 variant with two amino acid substitutions: an aspartic acid instead of a glycine at position 157 and a serine instead of a phenylalanine at position 153. The G157D mutation, present in OXA-14, is associated with the resistance of P. aeruginosa to ceftazidime. Compared to OXA-14, OXA-935 showed increased catalytic efficiency for ceftazidime. The deletion of blaOXA-935 restored the sensitivity to ceftazidime, and susceptibility profiling of P. aeruginosa laboratory strains expressing blaOXA-935 revealed that OXA-935 conferred ceftazidime resistance. To better understand the impacts of the variant amino acids, we determined the crystal structures of OXA-14 and OXA-935. Compared to OXA-14, the F153S mutation in OXA-935 conferred increased flexibility in the omega (X) loop. Amino acid changes that confer extended spectrum cephalosporinase activity to OXA-10-family b-lactamases are concerning, given the rising reliance on novel b-lactam/b-lactamase inhibitor combinations, such as ceftolozane-tazobactam and ceftazidime-avibactam, to treat MDR P. aeruginosa infections.",

keywords = "OXA-b-lactamase, Pseudomonas aeruginosa, antimicrobial resistance, ceftazidime, crystal structure",

author = "Pincus, {Nathan B.} and Monica Rosas-Lemus and Gatesy, {Samuel W.M.} and Bertucci, {Hanna K.} and Brunzelle, {Joseph S} and George Minasov and Shuvalova, {Ludmilla A.} and Marine Lebrun-Corbin and Satchell, {Karla J.F.} and Ozer, {Egon A.} and Hauser, {Alan R} and Bachta, {Kelly E.R.}",

note = "Funding Information: This work was supported by grants from the National Institutes of Health (NIH)/National Institute of Allergy and Infectious Diseases (NIAID) (R01 AI118257, R01 AI053674, U19 AI135964, K24 104831, and R21 AI129167 awarded to A.R.H.), the NIH/National Institute of General Medical Sciences (NIGMS) (T32 GM008061 and T32 GM008152 awarded to N.B.P.), an American Cancer Society (ACS) Postdoctoral Fellowship (number 130602-PF-17-107-01- MPC, awarded to K.E.R.B.), and an ACS Clinician Scientist Development Grant (number 134251-CSDG-20-053-01-MPC, awarded to K.E.R.B.). This project has been funded in whole or in part with federal funds from the NIAID under Contract No. HHSN27201700060C and Grant No. U01AI124316 and R01 GM05789 as well as from the National Institute of Medical Sciences (Grant GM118187), both from the NIH, Department of Health and Human Services. This work used the resources of the Advanced Photon Source, a U.S. Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory under Contract No. DE-AC02-06CH11357. Use of the LS-CAT Sector 21 was supported by the Michigan Economic Development Corporation and the Michigan Technology Tri-Corridor (Grant 085P1000817). This work was also supported by the Northwestern University NUSeq Core Facility, Structural Biology Facility, and High Throughput Analysis Laboratory, which are supported in part by the NCI CCSG P30 CA060553 award to the Robert H. Lurie Comprehensive Cancer Center. This work was also supported in part through the computational resources and staff contributions provided by the Genomics Compute Cluster, which is jointly supported by the Feinberg School of Medicine, the Center for Genetic Medicine, and Feinberg{\textquoteright}s Department of Biochemistry and Molecular Genetics, Office of the Provost, Office for Research, and Northwestern Information Technology. The Genomics Compute Cluster is part of Quest, Northwestern University{\textquoteright}s high-performance computing facility, and serves the purpose of advancing research in genomics. The funders had no role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript. We thank members of the Center for Structural Genomics of Infectious Diseases (CSGID) and the Hauser, Ozer, and Kociolek laboratories for their valuable comments during numerous discussions of this work. Funding Information: This work was supported by grants from the National Institutes of Health (NIH)/National Institute of Allergy and Infectious Diseases (NIAID) (R01 AI118257, R01 AI053674, U19 AI135964, K24 104831, and R21 AI129167 awarded to A.R.H.), the NIH/National Institute of General Medical Sciences (NIGMS) (T32 GM008061 and T32 GM008152 awarded to N.B.P.), an American Cancer Society (ACS) Postdoctoral Fellowship (number 130602-PF-17-107-01-MPC, awarded to K.E.R.B.), and an ACS Clinician Scientist Development Grant (number 134251-CSDG-20-053-01-MPC, awarded to K.E.R.B.). This project has been funded in whole or in part with federal funds from the NIAID under Contract No. HHSN27201700060C and Grant No. U01AI124316 and R01 GM05789 as well as from the National Institute of Medical Sciences (Grant GM118187), both from the NIH, Department of Health and Human Services. This work used the resources of the Advanced Photon Source, a U.S. Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory under Contract No. DE-AC02-06CH11357. Use of the LS-CAT Sector 21 was supported by the Michigan Economic Development Corporation and the Michigan Technology Tri-Corridor (Grant 085P1000817). This work was also supported by the Northwestern University NUSeq Core Facility, Structural Biology Facility, and High Throughput Analysis Laboratory, which are supported in part by the NCI CCSG P30 CA060553 award to the Robert H. Lurie Comprehensive Cancer Center. This work was also supported in part through the computational resources and staff contributions provided by the Genomics Compute Cluster, which is jointly supported by the Feinberg School of Medicine, the Center for Genetic Medicine, and Feinberg's Department of Biochemistry and Molecular Genetics, Office of the Provost, Office for Research, and Northwestern Information Technology. The Genomics Compute Cluster is part of Quest, Northwestern University's high-performance computing facility, and serves the purpose of advancing research in genomics. The funders had no role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript. We thank members of the Center for Structural Genomics of Infectious Diseases (CSGID) and the Hauser, Ozer, and Kociolek laboratories for their valuable comments during numerous discussions of this work. Publisher Copyright: Copyright {\textcopyright} 2022 Pincus et al.",

year = "2022",

month = oct,

doi = "10.1128/aac.00985-22",

language = "English (US)",

volume = "66",

journal = "Antimicrobial agents and chemotherapy",

issn = "0066-4804",

publisher = "American Society for Microbiology",

number = "10",

}

Pincus, NB, Rosas-Lemus, M, Gatesy, SWM, Bertucci, HK, Brunzelle, JS, Minasov, G , Shuvalova, LA, Lebrun-Corbin, M, Satchell, KJF , Ozer, EA , Hauser, AR & Bachta, KER 2022, 'Functional and Structural Characterization of OXA-935, a Novel OXA-10-Family β-Lactamase from Pseudomonas aeruginosa', Antimicrobial agents and chemotherapy, vol. 66, no. 10. https://doi.org/10.1128/aac.00985-22

TY - JOUR

T1 - Functional and Structural Characterization of OXA-935, a Novel OXA-10-Family β-Lactamase from Pseudomonas aeruginosa

AU - Pincus, Nathan B.

AU - Rosas-Lemus, Monica

AU - Gatesy, Samuel W.M.

AU - Bertucci, Hanna K.

AU - Brunzelle, Joseph S

AU - Minasov, George

AU - Shuvalova, Ludmilla A.

AU - Lebrun-Corbin, Marine

AU - Satchell, Karla J.F.

AU - Ozer, Egon A.

AU - Hauser, Alan R

AU - Bachta, Kelly E.R.

N1 - Funding Information: This work was supported by grants from the National Institutes of Health (NIH)/National Institute of Allergy and Infectious Diseases (NIAID) (R01 AI118257, R01 AI053674, U19 AI135964, K24 104831, and R21 AI129167 awarded to A.R.H.), the NIH/National Institute of General Medical Sciences (NIGMS) (T32 GM008061 and T32 GM008152 awarded to N.B.P.), an American Cancer Society (ACS) Postdoctoral Fellowship (number 130602-PF-17-107-01- MPC, awarded to K.E.R.B.), and an ACS Clinician Scientist Development Grant (number 134251-CSDG-20-053-01-MPC, awarded to K.E.R.B.). This project has been funded in whole or in part with federal funds from the NIAID under Contract No. HHSN27201700060C and Grant No. U01AI124316 and R01 GM05789 as well as from the National Institute of Medical Sciences (Grant GM118187), both from the NIH, Department of Health and Human Services. This work used the resources of the Advanced Photon Source, a U.S. Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory under Contract No. DE-AC02-06CH11357. Use of the LS-CAT Sector 21 was supported by the Michigan Economic Development Corporation and the Michigan Technology Tri-Corridor (Grant 085P1000817). This work was also supported by the Northwestern University NUSeq Core Facility, Structural Biology Facility, and High Throughput Analysis Laboratory, which are supported in part by the NCI CCSG P30 CA060553 award to the Robert H. Lurie Comprehensive Cancer Center. This work was also supported in part through the computational resources and staff contributions provided by the Genomics Compute Cluster, which is jointly supported by the Feinberg School of Medicine, the Center for Genetic Medicine, and Feinberg’s Department of Biochemistry and Molecular Genetics, Office of the Provost, Office for Research, and Northwestern Information Technology. The Genomics Compute Cluster is part of Quest, Northwestern University’s high-performance computing facility, and serves the purpose of advancing research in genomics. The funders had no role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript. We thank members of the Center for Structural Genomics of Infectious Diseases (CSGID) and the Hauser, Ozer, and Kociolek laboratories for their valuable comments during numerous discussions of this work. Funding Information: This work was supported by grants from the National Institutes of Health (NIH)/National Institute of Allergy and Infectious Diseases (NIAID) (R01 AI118257, R01 AI053674, U19 AI135964, K24 104831, and R21 AI129167 awarded to A.R.H.), the NIH/National Institute of General Medical Sciences (NIGMS) (T32 GM008061 and T32 GM008152 awarded to N.B.P.), an American Cancer Society (ACS) Postdoctoral Fellowship (number 130602-PF-17-107-01-MPC, awarded to K.E.R.B.), and an ACS Clinician Scientist Development Grant (number 134251-CSDG-20-053-01-MPC, awarded to K.E.R.B.). This project has been funded in whole or in part with federal funds from the NIAID under Contract No. HHSN27201700060C and Grant No. U01AI124316 and R01 GM05789 as well as from the National Institute of Medical Sciences (Grant GM118187), both from the NIH, Department of Health and Human Services. This work used the resources of the Advanced Photon Source, a U.S. Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory under Contract No. DE-AC02-06CH11357. Use of the LS-CAT Sector 21 was supported by the Michigan Economic Development Corporation and the Michigan Technology Tri-Corridor (Grant 085P1000817). This work was also supported by the Northwestern University NUSeq Core Facility, Structural Biology Facility, and High Throughput Analysis Laboratory, which are supported in part by the NCI CCSG P30 CA060553 award to the Robert H. Lurie Comprehensive Cancer Center. This work was also supported in part through the computational resources and staff contributions provided by the Genomics Compute Cluster, which is jointly supported by the Feinberg School of Medicine, the Center for Genetic Medicine, and Feinberg's Department of Biochemistry and Molecular Genetics, Office of the Provost, Office for Research, and Northwestern Information Technology. The Genomics Compute Cluster is part of Quest, Northwestern University's high-performance computing facility, and serves the purpose of advancing research in genomics. The funders had no role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript. We thank members of the Center for Structural Genomics of Infectious Diseases (CSGID) and the Hauser, Ozer, and Kociolek laboratories for their valuable comments during numerous discussions of this work. Publisher Copyright: Copyright © 2022 Pincus et al.

PY - 2022/10

Y1 - 2022/10

N2 - Resistance to antipseudomonal penicillins and cephalosporins is often driven by the overproduction of the intrinsic b-lactamase AmpC. However, OXA-10-family b-lactamases are a rich source of resistance in Pseudomonas aeruginosa. OXA b-lactamases have a propensity for mutation that leads to extended spectrum cephalosporinase and carbapenemase activity. In this study, we identified isolates from a subclade of the multidrug-resistant (MDR) high risk P. aeruginosa clonal complex CC446 with a resistance to ceftazidime. A genomic analysis revealed that these isolates harbored a plasmid containing a novel allele of blaOXA-10, named blaOXA-935, which was predicted to produce an OXA-10 variant with two amino acid substitutions: an aspartic acid instead of a glycine at position 157 and a serine instead of a phenylalanine at position 153. The G157D mutation, present in OXA-14, is associated with the resistance of P. aeruginosa to ceftazidime. Compared to OXA-14, OXA-935 showed increased catalytic efficiency for ceftazidime. The deletion of blaOXA-935 restored the sensitivity to ceftazidime, and susceptibility profiling of P. aeruginosa laboratory strains expressing blaOXA-935 revealed that OXA-935 conferred ceftazidime resistance. To better understand the impacts of the variant amino acids, we determined the crystal structures of OXA-14 and OXA-935. Compared to OXA-14, the F153S mutation in OXA-935 conferred increased flexibility in the omega (X) loop. Amino acid changes that confer extended spectrum cephalosporinase activity to OXA-10-family b-lactamases are concerning, given the rising reliance on novel b-lactam/b-lactamase inhibitor combinations, such as ceftolozane-tazobactam and ceftazidime-avibactam, to treat MDR P. aeruginosa infections.

AB - Resistance to antipseudomonal penicillins and cephalosporins is often driven by the overproduction of the intrinsic b-lactamase AmpC. However, OXA-10-family b-lactamases are a rich source of resistance in Pseudomonas aeruginosa. OXA b-lactamases have a propensity for mutation that leads to extended spectrum cephalosporinase and carbapenemase activity. In this study, we identified isolates from a subclade of the multidrug-resistant (MDR) high risk P. aeruginosa clonal complex CC446 with a resistance to ceftazidime. A genomic analysis revealed that these isolates harbored a plasmid containing a novel allele of blaOXA-10, named blaOXA-935, which was predicted to produce an OXA-10 variant with two amino acid substitutions: an aspartic acid instead of a glycine at position 157 and a serine instead of a phenylalanine at position 153. The G157D mutation, present in OXA-14, is associated with the resistance of P. aeruginosa to ceftazidime. Compared to OXA-14, OXA-935 showed increased catalytic efficiency for ceftazidime. The deletion of blaOXA-935 restored the sensitivity to ceftazidime, and susceptibility profiling of P. aeruginosa laboratory strains expressing blaOXA-935 revealed that OXA-935 conferred ceftazidime resistance. To better understand the impacts of the variant amino acids, we determined the crystal structures of OXA-14 and OXA-935. Compared to OXA-14, the F153S mutation in OXA-935 conferred increased flexibility in the omega (X) loop. Amino acid changes that confer extended spectrum cephalosporinase activity to OXA-10-family b-lactamases are concerning, given the rising reliance on novel b-lactam/b-lactamase inhibitor combinations, such as ceftolozane-tazobactam and ceftazidime-avibactam, to treat MDR P. aeruginosa infections.

KW - OXA-b-lactamase

KW - Pseudomonas aeruginosa

KW - antimicrobial resistance

KW - ceftazidime

KW - crystal structure

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U2 - 10.1128/aac.00985-22

DO - 10.1128/aac.00985-22

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C2 - 36129295

AN - SCOPUS:85140255400

SN - 0066-4804

VL - 66

JO - Antimicrobial agents and chemotherapy

JF - Antimicrobial agents and chemotherapy

IS - 10

ER -

Functional and Structural Characterization of OXA-935, a Novel OXA-10-Family β-Lactamase from Pseudomonas aeruginosa

Abstract

Funding

Keywords

ASJC Scopus subject areas

Access to Document

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Fingerprint

Crystal Structure of the Class D Beta-lactamase OXA-935 from Pseudomonas aeruginosa, Orthorhombic Crystal Form

Crystal Structure of the Oxacillin-hydrolyzing Class D Extended-spectrum Beta-lactamase OXA-14 from Pseudomonas aeruginosa

Crystal Structure of the Class D Beta-lactamase OXA-935 from Pseudomonas aeruginosa, Monoclinic Crystal Form

Cite this

Functional and Structural Characterization of OXA-935, a Novel OXA-10-Family β-Lactamase from Pseudomonas aeruginosa

Abstract

Funding

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Datasets

Crystal Structure of the Class D Beta-lactamase OXA-935 from Pseudomonas aeruginosa, Orthorhombic Crystal Form

Crystal Structure of the Oxacillin-hydrolyzing Class D Extended-spectrum Beta-lactamase OXA-14 from Pseudomonas aeruginosa

Crystal Structure of the Class D Beta-lactamase OXA-935 from Pseudomonas aeruginosa, Monoclinic Crystal Form

Cite this