› 1gs6

X-ray diffraction
2.2Å resolution

Crystal structure of M144A mutant of Alcaligenes xylosoxidans Nitrite Reductase

Released:
DOI: 10.2210/pdb1gs6/pdb
PDB entry 1gs6 coloured by chain, front view.
PDB entry 1gs6 coloured by chain, side view.
PDB entry 1gs6 coloured by chain, top view.
Source organism: Achromobacter xylosoxidans
Primary publication:
Biochemical and crystallographic studies of the Met144Ala, Asp92Asn and His254Phe mutants of the nitrite reductase from Alcaligenes xylosoxidans provide insight into the enzyme mechanism.
Ellis MJ, Prudêncio M, Dodd FE, Strange RW, Sawers G, Eady RR, Hasnain SS
J Mol Biol 316 51-64 (2002)
PMID: 11829502

Function and Biology Details

Reaction catalysed: 
Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130622 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chain: X
Molecule details ›
Chain: X
Length: 336 amino acids
Theoretical weight: 36.51 KDa
Source organism: Achromobacter xylosoxidans
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O68601 (Residues: 25-360; Coverage: 100%)
Gene names: O9570_16215, nir, nirK
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

2 bound ligands:
Ligand CU 2 x CU
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P63
Unit cell:
a: 106.86Å b: 106.86Å c: 64.026Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.15 0.148 0.181
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Recent structural insights into the function of copper nitrite reductases.
Horrell et al. (2017)
2 more

2 mentions without citation

3(10) helices in channels and other membrane proteins.
Vieira-Pires et al. (2010)
1 more