› 2dyu

X-ray diffraction
1.75Å resolution

Helicobacter pylori formamidase AmiF contains a fine-tuned cysteine-glutamate-lysine catalytic triad

Released:
DOI: 10.2210/pdb2dyu/pdb
PDB entry 2dyu coloured by chain, front view.
PDB entry 2dyu coloured by chain, side view.
PDB entry 2dyu coloured by chain, top view.
Source organism: Helicobacter pylori 26695
Primary publication:
Crystal structure of Helicobacter pylori formamidase AmiF reveals a cysteine-glutamate-lysine catalytic triad.
Hung CL, Liu JH, Chiu WC, Huang SW, Hwang JK, Wang WC
J Biol Chem 282 12220-9 (2007)
PMID: 17307742

Function and Biology Details

Reaction catalysed: 
Formamide + H(2)O = formate + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127791 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Formamidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 334 amino acids
Theoretical weight: 37.33 KDa
Source organism: Helicobacter pylori 26695
Expression system: Escherichia coli
UniProt:
  • Canonical: O25836 (Residues: 1-334; Coverage: 100%)
Gene names: HP_1238, amiF
Sequence domains: Carbon-nitrogen hydrolase
Structure domains: Carbon-nitrogen hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL12B2
Spacegroup: R3
Unit cell:
a: 147.215Å b: 147.215Å c: 72.273Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.174 0.215
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Primary or secondary? Versatile nitrilases in plant metabolism.
Piotrowski M. (2008)
3 more

3 mentions without citation

The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning.
Weber et al. (2013)
2 more