1R57

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

Summary for 1R57

• Entry DOI: 10.2210/pdb1r57/pdb
• NMR Information: BMRB: 5845
• Descriptor: conserved hypothetical protein (1 entity in total)
• Functional Keywords: gcn5, n-acetyltransferase, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, transferase
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 11631.88

Authors

Cort, J.R.,Acton, T.B.,Ma, L.,Xiao, R.B.,Montelione, G.T.,Kennedy, M.A.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2003-10-09, release date: 2004-03-09, Last modification date: 2024-05-01)

Primary citation

Cort, J.R.,Ramelot, T.A.,Murray, D.,Acton, T.B.,Ma, L.C.,Xiao, R.,Montelione, G.T.,Kennedy, M.A.
Structure of an acetyl-CoA binding protein from Staphylococcus aureus representing a novel subfamily of GCN5-related N-acetyltransferase-like proteins.
J.STRUCT.FUNCT.GENOM., 9:7-20, 2008

PubMed 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 macromolecule, such as another protein, or that a second protein subunit providing a substrate-binding region must combine with SACOL2532 to make a fully functional N-acetyl transferase.

PubMed: 18709443
DOI: 10.1007/s10969-008-9041-z

Experimental method

SOLUTION NMR