1R57

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


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 30 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with fewest restraint violations and lowest energy 

wwPDB Validation   3D Report Full Report


This is version 2.0 of the entry. See complete history


Literature

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

Cort, J.R.Ramelot, T.A.Murray, D.Acton, T.B.Ma, L.C.Xiao, R.Montelione, G.T.Kennedy, M.A.

(2008) J Struct Funct Genomics 9: 7-20

  • DOI: https://doi.org/10.1007/s10969-008-9041-z
  • Primary Citation of Related Structures:  
    1R57, 2H5M

  • 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.


  • Organizational Affiliation

    Washington State University Tri-Cities, Richland, WA 99354, USA, john.cort@pnl.gov


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
conserved hypothetical protein102Staphylococcus aureusMutation(s): 0 
Gene Names: SA2309 or MW2441 or SAV2521
EC: 2.3.1
UniProt
Find proteins for A0A0H3JTC0 (Staphylococcus aureus (strain Mu50 / ATCC 700699))
Explore A0A0H3JTC0 
Go to UniProtKB:  A0A0H3JTC0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0H3JTC0
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 30 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with fewest restraint violations and lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-03-09
    Type: Initial release
  • Version 1.1: 2007-12-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 2.0: 2019-11-06
    Changes: Data collection, Database references, Derived calculations, Polymer sequence