Structural, functional, and inhibition studies of a Gcn5-related N-acetyltransferase (GNAT) superfamily protein PA4794: A new C-terminal lysine protein acetyltransferase from pseudomonas aeruginosa

Karolina A. Majorek; Misty L. Kuhn; Maksymilian Chruszcz; Wayne F. Anderson; Wladek Minor

doi:10.1074/jbc.M113.501353

Structural, functional, and inhibition studies of a Gcn5-related N-acetyltransferase (GNAT) superfamily protein PA4794: A new C-terminal lysine protein acetyltransferase from pseudomonas aeruginosa

Karolina A. Majorek, Misty L. Kuhn, Maksymilian Chruszcz, Wayne F. Anderson, Wladek Minor^*

^*Corresponding author for this work

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

33 Scopus citations

Abstract

Background: Gcn5-related N-acetyltransferases (GNATs) are involved in small molecule and protein acetylation in all organisms. Results: Crystallographic and biochemical characterization of PA4794 is shown, including identification of substrates and inhibitors. Conclusion: PA4794 is a new bacterial C-terminal lysine protein acetyltransferase inhibited by cephalosporins. Significance: PA4794 is the first identified acetyltransferase specific for C-terminal lysine; identified interactions with cephalosporins may be of clinical relevance.

Original language	English (US)
Pages (from-to)	30223-30235
Number of pages	13
Journal	Journal of Biological Chemistry
Volume	288
Issue number	42
DOIs	https://doi.org/10.1074/jbc.M113.501353
State	Published - Oct 18 2013

Funding

ASJC Scopus subject areas

Molecular Biology
Biochemistry
Cell Biology

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10.1074/jbc.M113.501353

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Majorek, K. A., Kuhn, M. L., Chruszcz, M., Anderson, W. F., & Minor, W. (2013). Structural, functional, and inhibition studies of a Gcn5-related N-acetyltransferase (GNAT) superfamily protein PA4794: A new C-terminal lysine protein acetyltransferase from pseudomonas aeruginosa. Journal of Biological Chemistry, 288(42), 30223-30235. https://doi.org/10.1074/jbc.M113.501353

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title = "Structural, functional, and inhibition studies of a Gcn5-related N-acetyltransferase (GNAT) superfamily protein PA4794: A new C-terminal lysine protein acetyltransferase from pseudomonas aeruginosa",

abstract = "Background: Gcn5-related N-acetyltransferases (GNATs) are involved in small molecule and protein acetylation in all organisms. Results: Crystallographic and biochemical characterization of PA4794 is shown, including identification of substrates and inhibitors. Conclusion: PA4794 is a new bacterial C-terminal lysine protein acetyltransferase inhibited by cephalosporins. Significance: PA4794 is the first identified acetyltransferase specific for C-terminal lysine; identified interactions with cephalosporins may be of clinical relevance.",

author = "Majorek, {Karolina A.} and Kuhn, {Misty L.} and Maksymilian Chruszcz and Anderson, {Wayne F.} and Wladek Minor",

year = "2013",

month = oct,

day = "18",

doi = "10.1074/jbc.M113.501353",

language = "English (US)",

volume = "288",

pages = "30223--30235",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

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Majorek, KA, Kuhn, ML, Chruszcz, M, Anderson, WF & Minor, W 2013, 'Structural, functional, and inhibition studies of a Gcn5-related N-acetyltransferase (GNAT) superfamily protein PA4794: A new C-terminal lysine protein acetyltransferase from pseudomonas aeruginosa', Journal of Biological Chemistry, vol. 288, no. 42, pp. 30223-30235. https://doi.org/10.1074/jbc.M113.501353

Structural, functional, and inhibition studies of a Gcn5-related N-acetyltransferase (GNAT) superfamily protein PA4794: A new C-terminal lysine protein acetyltransferase from pseudomonas aeruginosa. / Majorek, Karolina A.; Kuhn, Misty L.; Chruszcz, Maksymilian et al.
In: Journal of Biological Chemistry, Vol. 288, No. 42, 18.10.2013, p. 30223-30235.

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

TY - JOUR

T1 - Structural, functional, and inhibition studies of a Gcn5-related N-acetyltransferase (GNAT) superfamily protein PA4794

T2 - A new C-terminal lysine protein acetyltransferase from pseudomonas aeruginosa

AU - Majorek, Karolina A.

AU - Kuhn, Misty L.

AU - Chruszcz, Maksymilian

AU - Anderson, Wayne F.

AU - Minor, Wladek

PY - 2013/10/18

Y1 - 2013/10/18

N2 - Background: Gcn5-related N-acetyltransferases (GNATs) are involved in small molecule and protein acetylation in all organisms. Results: Crystallographic and biochemical characterization of PA4794 is shown, including identification of substrates and inhibitors. Conclusion: PA4794 is a new bacterial C-terminal lysine protein acetyltransferase inhibited by cephalosporins. Significance: PA4794 is the first identified acetyltransferase specific for C-terminal lysine; identified interactions with cephalosporins may be of clinical relevance.

AB - Background: Gcn5-related N-acetyltransferases (GNATs) are involved in small molecule and protein acetylation in all organisms. Results: Crystallographic and biochemical characterization of PA4794 is shown, including identification of substrates and inhibitors. Conclusion: PA4794 is a new bacterial C-terminal lysine protein acetyltransferase inhibited by cephalosporins. Significance: PA4794 is the first identified acetyltransferase specific for C-terminal lysine; identified interactions with cephalosporins may be of clinical relevance.

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Structural, functional, and inhibition studies of a Gcn5-related N-acetyltransferase (GNAT) superfamily protein PA4794: A new C-terminal lysine protein acetyltransferase from pseudomonas aeruginosa

Abstract

Funding

ASJC Scopus subject areas

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Crystal structure of PA4794 - GNAT superfamily protein in complex with AcCoA

Crystal structure of a GNAT superfamily acetyltransferase PA4794 in complex with Cefoxitin

Crystal structure of a GNAT superfamily acetyltransferase PA4794 in complex with Cefalotin

Cite this

Structural, functional, and inhibition studies of a Gcn5-related N-acetyltransferase (GNAT) superfamily protein PA4794: A new C-terminal lysine protein acetyltransferase from pseudomonas aeruginosa

Abstract

Funding

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Datasets

Crystal structure of PA4794 - GNAT superfamily protein in complex with AcCoA

Crystal structure of a GNAT superfamily acetyltransferase PA4794 in complex with Cefoxitin

Crystal structure of a GNAT superfamily acetyltransferase PA4794 in complex with Cefalotin

Cite this