› 6qq0

X-ray diffraction
1.4Å resolution

Crystal structure of nitrite bound Y323E mutant of haem-Cu containing nitrite reductase from Ralstonia pickettii

Released:
DOI: 10.2210/pdb6qq0/pdb
PDB entry 6qq0 coloured by chain, front view.
PDB entry 6qq0 coloured by chain, side view.
PDB entry 6qq0 coloured by chain, top view.
Source organism: Ralstonia pickettii
Primary publication:
Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis.
Hedison TM, Shenoy RT, Iorgu AI, Heyes DJ, Fisher K, Wright GSA, Hay S, Eady RR, Antonyuk SV, Hasnain SS, Scrutton NS
ACS Catal 9 6087-6099 (2019)
PMID: 32051772

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 analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125137 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-containing nitrite reductase Chain: A
Molecule details ›
Chain: A
Length: 468 amino acids
Theoretical weight: 49.91 KDa
Source organism: Ralstonia pickettii
Expression system: Escherichia coli
UniProt:
  • Canonical: I6NAW4 (Residues: 32-499; Coverage: 100%)
Gene names: D7S62_04310, nirK
Sequence domains:

Ligands and Environments


Cofactor: Ligand HEC 1 x HEC
3 bound ligands:
Ligand CU 2 x CU
Ligand NO2 1 x NO2
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: R3
Unit cell:
a: 127.65Å b: 127.65Å c: 86.56Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.115 0.113 0.146
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Catalytically important damage-free structures of a copper nitrite reductase obtained by femtosecond X-ray laser and room-temperature neutron crystallography.
Halsted et al. (2019)
7 more

1 mention without citation

Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis.
Hedison et al. (2019)