› 1tiq

X-ray diffraction
1.9Å resolution

Crystal Structure of an Acetyltransferase (PaiA) in complex with CoA and DTT from Bacillus subtilis, Northeast Structural Genomics Target SR64.

Released:
DOI: 10.2210/pdb1tiq/pdb
PDB entry 1tiq coloured by chain, front view.
PDB entry 1tiq coloured by chain, side view.
PDB entry 1tiq coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structural and functional evidence for Bacillus subtilis PaiA as a novel N1-spermidine/spermine acetyltransferase.
Forouhar F, Lee IS, Vujcic J, Vujcic S, Shen J, Vorobiev SM, Xiao R, Acton TB, Montelione GT, Porter CW, Tong L
J Biol Chem 280 40328-36 (2005)
PMID: 16210326

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149211 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Spermidine/spermine N(1)-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 180 amino acids
Theoretical weight: 21.44 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P21340 (Residues: 1-172; Coverage: 100%)
Gene names: BSU32150, paiA
Sequence domains: Acetyltransferase (GNAT) domain
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand COA 3 x COA
2 bound ligands:
Ligand DTT 2 x DTT
Ligand SO4 1 x SO4
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2221
Unit cell:
a: 39.87Å b: 135.825Å c: 132.395Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.241
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Spermidine/spermine-N(1)-acetyltransferase: a key metabolic regulator.
Pegg AE. (2008)
3 more

12 mentions without citation

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