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PDBsum entry 4klv

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protein ligands links
Transferase PDB id
4klv
Jmol
Contents
Protein chain
159 a.a.
Ligands
SO4 ×7
EDO ×11
KLV
Waters ×240
PDB id:
4klv
Name: Transferase
Title: Crystal structure of a gnat superfamily acetyltransferase pa complex with 4-methylumbelliferyl phosphate
Structure: Uncharacterized protein. Chain: a. Engineered: yes
Source: Pseudomonas aeruginosa. Organism_taxid: 208964. Strain: pao1. Gene: pa4794. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.30Å     R-factor:   0.124     R-free:   0.152
Authors: K.A.Majorek,M.Chruszcz,A.Joachimiak,W.Minor,Midwest Center F Structural Genomics (Mcsg)
Key ref: K.A.Majorek et al. (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. J Biol Chem, 288, 30223-30235. PubMed id: 24003232 DOI: 10.1074/jbc.M113.501353
Date:
07-May-13     Release date:   22-May-13    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9HV14  (Q9HV14_PSEAE) -  Uncharacterized protein
Seq:
Struc:
160 a.a.
159 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     N-acetyltransferase activity     1 term  

 

 
DOI no: 10.1074/jbc.M113.501353 J Biol Chem 288:30223-30235 (2013)
PubMed id: 24003232  
 
 
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.
K.A.Majorek, M.L.Kuhn, M.Chruszcz, W.F.Anderson, W.Minor.
 
  ABSTRACT  
 
The Gcn5-related N-acetyltransferase (GNAT) superfamily is a large group of evolutionarily related acetyltransferases, with multiple paralogs in organisms from all kingdoms of life. The functionally characterized GNATs have been shown to catalyze the transfer of an acetyl group from acetyl-coenzyme A (Ac-CoA) to the amine of a wide range of substrates, including small molecules and proteins. GNATs are prevalent and implicated in a myriad of aspects of eukaryotic and prokaryotic physiology, but functions of many GNATs remain unknown. In this work, we used a multi-pronged approach of x-ray crystallography and biochemical characterization to elucidate the sequence-structure-function relationship of the GNAT superfamily member PA4794 from Pseudomonas aeruginosa. We determined that PA4794 acetylates the Nε amine of a C-terminal lysine residue of a peptide, suggesting it is a protein acetyltransferase specific for a C-terminal lysine of a substrate protein or proteins. Furthermore, we identified a number of molecules, including cephalosporin antibiotics, which are inhibitors of PA4794 and bind in its substrate-binding site. Often, these molecules mimic the conformation of the acetylated peptide product. We have determined structures of PA4794 in the apo-form, in complexes with Ac-CoA, CoA, several antibiotics and other small molecules, and a ternary complex with the products of the reaction: CoA and acetylated peptide. Also, we analyzed PA4794 mutants to identify residues important for substrate binding and catalysis.