› 2i6r

X-ray diffraction
2.51Å resolution

Crystal structure of E. coli HypE, a hydrogenase maturation protein

Released:
DOI: 10.2210/pdb2i6r/pdb
PDB entry 2i6r coloured by chain, front view.
PDB entry 2i6r coloured by chain, side view.
PDB entry 2i6r coloured by chain, top view.
Source organism: Escherichia coli O157:H7
Primary publication:
Structure of [NiFe] hydrogenase maturation protein HypE from Escherichia coli and its interaction with HypF.
Rangarajan ES, Asinas A, Proteau A, Munger C, Baardsnes J, Iannuzzi P, Matte A, Cygler M
J Bacteriol 190 1447-58 (2008)
PMID: 18065529

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150169 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbamoyl dehydratase HypE Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 334 amino acids
Theoretical weight: 35.14 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P24193 (Residues: 15-336; Coverage: 96%)
Gene names: JW2700, b2730, hypE
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: C2
Unit cell:
a: 254.757Å b: 71.776Å c: 113.034Å
α: 90° β: 115.12° γ: 90°
R-values:
R R work R free
0.193 0.193 0.24
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

Hydrogenases from methanogenic archaea, nickel, a novel cofactor, and H2 storage.
Thauer et al. (2010)
4 more