› 2e85

X-ray diffraction
1.7Å resolution

Crystal Structure of the Hydrogenase 3 Maturation protease

Released:
DOI: 10.2210/pdb2e85/pdb
PDB entry 2e85 coloured by chain, front view.
PDB entry 2e85 coloured by chain, side view.
PDB entry 2e85 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of hydrogenase maturating endopeptidase HycI from Escherichia coli.
Kumarevel T, Tanaka T, Bessho Y, Shinkai A, Yokoyama S
Biochem Biophys Res Commun 389 310-4 (2009)
PMID: 19720045

Function and Biology Details

Reaction catalysed: 
This enzyme specifically removes a 32-amino acid peptide from the C-terminus of the precursor of the large subunit of E.coli hydrogenase 3 by cleavage at the C-terminal side of Arg-537.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142508 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydrogenase 3 maturation protease Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 17.26 KDa
Source organism: Escherichia coli
Expression system: cell-free synthesis
UniProt:
  • Canonical: P0AEV9 (Residues: 1-156; Coverage: 100%)
Gene names: JW2687, b2717, hycI
Sequence domains: Hydrogenase maturation protease
Structure domains: HybD-like

Ligands and Environments

1 bound ligand:
Ligand CA 6 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P21212
Unit cell:
a: 87.425Å b: 54.984Å c: 67.964Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.248 0.258
Expression system: cell-free synthesis

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Citations

1 review citation

Microbial nickel proteins.
Kaluarachchi et al. (2010)
3 other articles