› 1n50

X-ray diffraction
2.9Å resolution

FOLLOWING THE C HEME REDUCTION IN NITRITE REDUCTASE FROM PSEUDOMONAS AERUGINOSA

Released:
DOI: 10.2210/pdb1n50/pdb
PDB entry 1n50 coloured by chain, front view.
PDB entry 1n50 coloured by chain, side view.
PDB entry 1n50 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Does the reduction of c heme trigger the conformational change of crystalline nitrite reductase?
Nurizzo D, Cutruzzolà F, Arese M, Bourgeois D, Brunori M, Cambillau C, Tegoni M
J Biol Chem 274 14997-5004 (1999)
PMID: 10329702

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 543 amino acids
Theoretical weight: 60.26 KDa
Source organism: Pseudomonas aeruginosa
UniProt:
  • Canonical: P24474 (Residues: 26-568; Coverage: 100%)
Gene names: PA0519, nirS
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEC 2 x HEC

Cofactor: Ligand DHE 2 x DHE
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21212
Unit cell:
a: 165.53Å b: 89.85Å c: 112.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.208 0.246

Quick links

Citations

10 citation in other articles

Redox-dependent conformational changes in cytochrome C oxidase suggest a gating mechanism for proton uptake.
Qin et al. (2009)
9 more

1 mention without citation

Pathogenicity of the BRCA1 missense variant M1775K is determined by the disruption of the BRCT phosphopeptide-binding pocket: a multi-modal approach.
Tischkowitz et al. (2008)