› 6qq6

Electron Microscopy
3.3Å resolution

Cryo-EM structure of dimeric quinol dependent nitric oxide reductase (qNOR) Val495Ala mutant from Alcaligenes xylosoxidans

Released:
DOI: 10.2210/pdb6qq6/pdb
PDB entry 6qq6 coloured by chain, front view.
PDB entry 6qq6 coloured by chain, side view.
PDB entry 6qq6 coloured by chain, top view.
Source organism: Achromobacter xylosoxidans
Primary publication:
Dimeric structures of quinol-dependent nitric oxide reductases (qNORs) revealed by cryo-electron microscopy.
Gopalasingam CC, Johnson RM, Chiduza GN, Tosha T, Yamamoto M, Shiro Y, Antonyuk SV, Muench SP, Hasnain SS
Sci Adv 5 eaax1803 (2019)
PMID: 31489376
Related structures: EMD-4619

Function and Biology Details

Reaction catalysed: 
Nitrous oxide + 2 ferricytochrome c + H(2)O = 2 nitric oxide + 2 ferrocytochrome c + 2 H(+)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101142 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitric oxide reductase subunit B Chains: A, B
Molecule details ›
Chains: A, B
Length: 746 amino acids
Theoretical weight: 83.09 KDa
Source organism: Achromobacter xylosoxidans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0D6H8R3 (Residues: 1-746; Coverage: 98%)
Gene names: ERS451415_02175, norB_1
Sequence domains: Cytochrome C and Quinol oxidase polypeptide I

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
4 bound ligands:
Ligand FE 2 x FE
Ligand CA 2 x CA
Ligand LOP 3 x LOP
Ligand LMT 2 x LMT
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.3Å
Relevant EMDB volumes: EMD-4619
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.
Reed et al. (2021)
4 other articles

1 mention without citation

The active form of quinol-dependent nitric oxide reductase from Neisseria meningitidis is a dimer.
Jamali et al. (2020)