2h5m | pdb_00002h5m

NMR Solution Structure of a GCN5-like putative N-acetyltransferase from Staphylococcus aureus complexed with acetyl-CoA. Northeast Structural Genomics Consortium Target ZR31

spinqualitylabelsall models 2h5m, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2h5m is a 1 chain structure with sequence from Staac. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACO Related: 1r57 Gene: SACOL2532 (STAAC) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed We have determined the solution NMR structure of SA(COL)2532, a putative GCN5-like N-acetyltransferase (GNAT) from Staphylococcus aureus. SA(COL)2532 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 macromolecule, such as another protein, or that a second protein subunit providing a substrate-binding region must combine with SA(COL)2532 to make a fully functional N-acetyl transferase. Structure of an acetyl-CoA binding protein from Staphylococcus aureus representing a novel subfamily of GCN5-related N-acetyltransferase-like proteins.,Cort JR, Ramelot TA, Murray D, Acton TB, Ma LC, Xiao R, Montelione GT, Kennedy MA J Struct Funct Genomics. 2008 Aug 16. PMID:18709443 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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