Structure of an acetyl-CoA binding protein from Staphylococcus aureus representing a novel subfamily of GCN5-related N-acetyltransferase-like proteins.

Journal of Structural and Functional Genomics
John R CortMichael A Kennedy

Abstract

We have determined the solution NMR structure of SACOL2532, a putative GCN5-like N-acetyltransferase (GNAT) from Staphylococcus aureus. SACOL2532 was shown to bind both CoA and acetyl-CoA, and structures with and without bound CoA were determined. Based on analysis of the structure and sequence, a subfamily of small GCN5-related N-acetyltransferase (GNAT)-like proteins can be defined. Proteins from this subfamily, which is largely congruent with COG2388, are characterized by a cysteine residue in the acetyl-CoA binding site near the acetyl group, by their small size in relation to other GNATs, by a lack of obvious substrate binding site, and by a distinct conformation of bound CoA in relation to other GNATs. Subfamily members are found in many bacterial and eukaryotic genomes, and in some archaeal genomes. Whereas other GNATs transfer the acetyl group of acetyl-CoA directly to an aliphatic amine, the presence of the conserved cysteine residue suggests that proteins in the COG2388 GNAT-subfamily transfer an acetyl group from acetyl-CoA to one or more presently unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The apparent absence of a substrate-binding region suggests that the substrate is a macromolecu...Continue Reading

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Citations

Jun 8, 2011·Insect Biochemistry and Molecular Biology·Prajwalini MehereJianyong Li
Jan 21, 2012·Microbiology·Gerald L NewtonMamta Rawat
Jul 8, 2020·Molecular Systems Biology·Willy V BienvenutIris Finkemeier
Feb 5, 2009·Proteins·Claudia BertonatiBurkhard Rost
Aug 26, 2020·Biochimica Et Biophysica Acta. Gene Regulatory Mechanisms·Brittany N Albaugh, John M Denu
Feb 3, 2021·Journal of Bacteriology·Anne TroitzschJan Pané-Farré

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