› 1xco

X-ray diffraction
2.85Å resolution

Crystal Structure of a Phosphotransacetylase from Bacillus subtilis in complex with acetylphosphate

Released:
DOI: 10.2210/pdb1xco/pdb
PDB entry 1xco coloured by chain, front view.
PDB entry 1xco coloured by chain, side view.
PDB entry 1xco coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Crystal structures of a phosphotransacetylase from Bacillus subtilis and its complex with acetyl phosphate.
Xu QS, Jancarik J, Lou Y, Kuznetsova K, Yakunin AF, Yokota H, Adams P, Kim R, Kim SH
J Struct Funct Genomics 6 269-79 (2005)
PMID: 16283428

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + phosphate = CoA + acetyl phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153920 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphate acetyltransferase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 329 amino acids
Theoretical weight: 35.17 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P39646 (Residues: 1-323; Coverage: 100%)
Gene names: BSU37660, ipa-88d, pta, ywfJ
Sequence domains: Phosphate acetyl/butaryl transferase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand UVW 23 x UVW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P6422
Unit cell:
a: 184.661Å b: 184.661Å c: 259.456Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.246 0.245 0.288
Expression system: Escherichia coli

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Citations

1 review citation

Structure and function of enzymes involved in the anaerobic degradation of L-threonine to propionate.
Simanshu et al. (2007)
12 other articles

4 mentions without citation

Structural, kinetic and proteomic characterization of acetyl phosphate-dependent bacterial protein acetylation.
Kuhn et al. (2014)
3 more