› 3ne7

X-ray diffraction
2.3Å resolution

Crystal structure of paia n-acetyltransferase from thermoplasma acidophilum in complex with coenzyme a

Released:
DOI: 10.2210/pdb3ne7/pdb
PDB entry 3ne7 coloured by chain, front view.
PDB entry 3ne7 coloured by chain, side view.
PDB entry 3ne7 coloured by chain, top view.
Source organism: Thermoplasma acidophilum
Primary publication:
Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production.
Filippova EV, Shuvalova L, Minasov G, Kiryukhina O, Zhang Y, Clancy S, Radhakrishnan I, Joachimiak A, Anderson WF
Proteins 79 2566-77 (2011)
PMID: 21633970

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190889 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Spermidine N(1)-acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 18.95 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9HL57 (Residues: 1-159; Coverage: 99%)
Gene names: Ta0374, paiA
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand COA 1 x COA
5 bound ligands:
Ligand NI 1 x NI
Ligand BME 2 x BME
Ligand SO4 1 x SO4
Ligand GOL 1 x GOL
Ligand UNL 1 x UNL
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P43212
Unit cell:
a: 69.224Å b: 69.224Å c: 90.628Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.184 0.238
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Bacterial GCN5-Related N-Acetyltransferases: From Resistance to Regulation.
Favrot et al. (2016)
1 more

4 mentions without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)
3 more