› 1hzv

X-ray diffraction
2.83Å resolution

DOMAIN SWING UPON HIS TO ALA MUTATION IN NITRITE REDUCTASE OF PSEUDOMONAS AERUGINOSA

Released:
DOI: 10.2210/pdb1hzv/pdb
PDB entry 1hzv coloured by chain, front view.
PDB entry 1hzv coloured by chain, side view.
PDB entry 1hzv coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Domain swing upon His to Ala mutation in nitrite reductase of Pseudomonas aeruginosa.
Brown K, Roig-Zamboni V, Cutruzzola' F, Arese M, Sun W, Brunori M, Cambillau C, Tegoni M
J Mol Biol 312 541-54 (2001)
PMID: 11563915

Function and Biology Details

Reactions catalysed: 
Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+)
NH(3) + H(2)O + acceptor = hydroxylamine + reduced acceptor
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150236 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitrite reductase Chain: A
Molecule details ›
Chain: A
Length: 543 amino acids
Theoretical weight: 60.19 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Pseudomonas putida
UniProt:
  • Canonical: P24474 (Residues: 26-568; Coverage: 100%)
Gene names: PA0519, nirS
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand DHE 1 x DHE

Cofactor: Ligand HEC 1 x HEC
1 bound ligand:
Ligand NO 1 x NO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14, ESRF BEAMLINE ID14-2
Spacegroup: P41212
Unit cell:
a: 94.744Å b: 94.744Å c: 159.901Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.286 0.282 0.296
Expression system: Pseudomonas putida

Quick links

Citations

1 review citation

Intramolecular electron transfer in nitrite reductases.
Wherland et al. (2005)
7 other articles

2 mentions without citation

The nitrite reductase from Pseudomonas aeruginosa: essential role of two active-site histidines in the catalytic and structural properties.
Cutruzzola et al. (2001)
1 more