› 1w2i

X-ray diffraction
1.5Å resolution

Crystal structuore of acylphosphatase from Pyrococcus horikoshii complexed with formate

Released:
DOI: 10.2210/pdb1w2i/pdb
PDB entry 1w2i coloured by chain, front view.
PDB entry 1w2i coloured by chain, side view.
PDB entry 1w2i coloured by chain, top view.
Source organism: Pyrococcus horikoshii
Primary publication:
Crystal structure of a hyperthermophilic archaeal acylphosphatase from Pyrococcus horikoshii--structural insights into enzymatic catalysis, thermostability, and dimerization.
Cheung YY, Lam SY, Chu WK, Allen MD, Bycroft M, Wong KB
Biochemistry 44 4601-11 (2005)
PMID: 15779887

Function and Biology Details

Reaction catalysed: 
An acylphosphate + H(2)O = a carboxylate + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160842 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acylphosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 91 amino acids
Theoretical weight: 10.28 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P84142 (Residues: 1-91; Coverage: 100%)
Gene names: PH0305.1, acyP
Sequence domains: Acylphosphatase
Structure domains: Alpha-Beta Plaits

Ligands and Environments

1 bound ligand:
Ligand FMT 4 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P3221
Unit cell:
a: 85.336Å b: 85.336Å c: 75.65Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.167 0.166 0.174
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

"Native-like aggregation" of the acylphosphatase from Sulfolobus solfataricus and its biological implications.
Bemporad et al. (2009)
20 other articles

3 mentions without citation

A rigidifying salt-bridge favors the activity of thermophilic enzyme at high temperatures at the expense of low-temperature activity.
Lam et al. (2011)
2 more