Structural characterization of a hypothetical protein: A potential agent involved in trimethylamine metabolism in Catenulispora acidiphila

Ekaterina V. Filippova; Chi Hao Luan; Sara F. Dunne; Olga Kiryukhina; George Minasov; Ludmilla Shuvalova; Wayne F. Anderson

doi:10.1007/s10969-014-9176-z

Structural characterization of a hypothetical protein: A potential agent involved in trimethylamine metabolism in Catenulispora acidiphila

Ekaterina V. Filippova, Chi Hao Luan, Sara F. Dunne, Olga Kiryukhina, George Minasov, Ludmilla Shuvalova, Wayne F. Anderson^*

^*Corresponding author for this work

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

7 Scopus citations

Abstract

Catenulispora acidiphila is a newly identified lineage of actinomycetes that produces antimicrobial activities and represents a promising source of novel antibiotics and secondary metabolites. Among the discovered protein coding genes, 68 % were assigned a putative function, while the remaining 32 % are genes encoding "hypothetical" proteins. Caci-0382 is one of the "hypothetical" proteins that has very few homologs. Sequence analysis shows that the protein belongs to the NTF2-like protein family. The structure of Caci-0382 demonstrates that it shares the same fold and has a similar active site as limonene-1,2-epoxide hydrolase, which suggests that it may have a related function. Using a fluorescence thermal shift assay, we identified stabilizing compounds that suggest potential natural ligands of Caci-0382. Using this information, we determined the crystal structure in complex with trimethylamine to provide a better understanding of the function of this uncharacterized protein.

Original language	English (US)
Pages (from-to)	33-40
Number of pages	8
Journal	Journal of Structural and Functional Genomics
Volume	15
Issue number	1
DOIs	https://doi.org/10.1007/s10969-014-9176-z
State	Published - Mar 2014

Funding

Acknowledgements The data collection was supported by the Argonne National Laboratory, at the Advanced Photon Source (APS), which is operated by University of Chicago Argonne, LLC, for the U.S. Department of Energy, Office of Biological and Environmental Research under contract DE-AC02-06CH11357. The authors would like to thank members of the LS-CAT at the APS for their help in the development of the Project. This study is supported by NIH PSI Grant GM074942 to the Midwest Center for Structural Genomics.

Keywords

Caci-0382
NTF2-like superfamily
Structural genomics
Trimethylamine
X-ray crystal structure

ASJC Scopus subject areas

Genetics
Structural Biology
Biochemistry

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10.1007/s10969-014-9176-z

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title = "Structural characterization of a hypothetical protein: A potential agent involved in trimethylamine metabolism in Catenulispora acidiphila",

abstract = "Catenulispora acidiphila is a newly identified lineage of actinomycetes that produces antimicrobial activities and represents a promising source of novel antibiotics and secondary metabolites. Among the discovered protein coding genes, 68 % were assigned a putative function, while the remaining 32 % are genes encoding {"}hypothetical{"} proteins. Caci-0382 is one of the {"}hypothetical{"} proteins that has very few homologs. Sequence analysis shows that the protein belongs to the NTF2-like protein family. The structure of Caci-0382 demonstrates that it shares the same fold and has a similar active site as limonene-1,2-epoxide hydrolase, which suggests that it may have a related function. Using a fluorescence thermal shift assay, we identified stabilizing compounds that suggest potential natural ligands of Caci-0382. Using this information, we determined the crystal structure in complex with trimethylamine to provide a better understanding of the function of this uncharacterized protein.",

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note = "Funding Information: Acknowledgements The data collection was supported by the Argonne National Laboratory, at the Advanced Photon Source (APS), which is operated by University of Chicago Argonne, LLC, for the U.S. Department of Energy, Office of Biological and Environmental Research under contract DE-AC02-06CH11357. The authors would like to thank members of the LS-CAT at the APS for their help in the development of the Project. This study is supported by NIH PSI Grant GM074942 to the Midwest Center for Structural Genomics.",

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AU - Kiryukhina, Olga

AU - Minasov, George

AU - Shuvalova, Ludmilla

AU - Anderson, Wayne F.

N1 - Funding Information: Acknowledgements The data collection was supported by the Argonne National Laboratory, at the Advanced Photon Source (APS), which is operated by University of Chicago Argonne, LLC, for the U.S. Department of Energy, Office of Biological and Environmental Research under contract DE-AC02-06CH11357. The authors would like to thank members of the LS-CAT at the APS for their help in the development of the Project. This study is supported by NIH PSI Grant GM074942 to the Midwest Center for Structural Genomics.

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N2 - Catenulispora acidiphila is a newly identified lineage of actinomycetes that produces antimicrobial activities and represents a promising source of novel antibiotics and secondary metabolites. Among the discovered protein coding genes, 68 % were assigned a putative function, while the remaining 32 % are genes encoding "hypothetical" proteins. Caci-0382 is one of the "hypothetical" proteins that has very few homologs. Sequence analysis shows that the protein belongs to the NTF2-like protein family. The structure of Caci-0382 demonstrates that it shares the same fold and has a similar active site as limonene-1,2-epoxide hydrolase, which suggests that it may have a related function. Using a fluorescence thermal shift assay, we identified stabilizing compounds that suggest potential natural ligands of Caci-0382. Using this information, we determined the crystal structure in complex with trimethylamine to provide a better understanding of the function of this uncharacterized protein.

AB - Catenulispora acidiphila is a newly identified lineage of actinomycetes that produces antimicrobial activities and represents a promising source of novel antibiotics and secondary metabolites. Among the discovered protein coding genes, 68 % were assigned a putative function, while the remaining 32 % are genes encoding "hypothetical" proteins. Caci-0382 is one of the "hypothetical" proteins that has very few homologs. Sequence analysis shows that the protein belongs to the NTF2-like protein family. The structure of Caci-0382 demonstrates that it shares the same fold and has a similar active site as limonene-1,2-epoxide hydrolase, which suggests that it may have a related function. Using a fluorescence thermal shift assay, we identified stabilizing compounds that suggest potential natural ligands of Caci-0382. Using this information, we determined the crystal structure in complex with trimethylamine to provide a better understanding of the function of this uncharacterized protein.

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Structural characterization of a hypothetical protein: A potential agent involved in trimethylamine metabolism in Catenulispora acidiphila

Abstract

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Keywords

ASJC Scopus subject areas

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Crystal structure of hypothetical protein with ketosteroid isomerase-like protein fold from Catenulispora acidiphila DSM 44928 in complex with Trimethylamine.

Crystal structure of hypothetical protein with ketosteroid isomerase-like protein fold from Catenulispora acidiphila DSM 44928

Cite this

Structural characterization of a hypothetical protein: A potential agent involved in trimethylamine metabolism in Catenulispora acidiphila

Abstract

Funding

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Datasets

Crystal structure of hypothetical protein with ketosteroid isomerase-like protein fold from Catenulispora acidiphila DSM 44928 in complex with Trimethylamine.

Crystal structure of hypothetical protein with ketosteroid isomerase-like protein fold from Catenulispora acidiphila DSM 44928

Cite this