› 2bs4

X-ray diffraction
2.76Å resolution

GLU C180 -> ILE VARIANT QUINOL:FUMARATE REDUCTASE FROMWOLINELLA SUCCINOGENES

Released:
DOI: 10.2210/pdb2bs4/pdb
PDB entry 2bs4 coloured by chain, front view.
PDB entry 2bs4 coloured by chain, side view.
PDB entry 2bs4 coloured by chain, top view.
Source organism: Wolinella succinogenes
Primary publication:
Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase.
Lancaster CR, Sauer US, Gross R, Haas AH, Graf J, Schwalbe H, Mäntele W, Simon J, Madej MG
Proc Natl Acad Sci U S A 102 18860-5 (2005)
PMID: 16380425

Function and Biology Details

Reaction catalysed: 
Succinate + a quinone = fumarate + a quinol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148052 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Fumarate reductase flavoprotein subunit Chains: A, D
Molecule details ›
Chains: A, D
Length: 656 amino acids
Theoretical weight: 72.83 KDa
Source organism: Wolinella succinogenes
UniProt:
  • Canonical: P17412 (Residues: 1-656; Coverage: 100%)
Gene names: WS0831, frdA
Sequence domains:
Structure domains:
Fumarate reductase iron-sulfur subunit Chains: B, E
Molecule details ›
Chains: B, E
Length: 239 amino acids
Theoretical weight: 27.2 KDa
Source organism: Wolinella succinogenes
UniProt:
  • Canonical: P17596 (Residues: 1-239; Coverage: 100%)
Gene names: WS0830, frdB
Sequence domains:
Structure domains:
Fumarate reductase cytochrome b subunit Chains: C, F
Molecule details ›
Chains: C, F
Length: 256 amino acids
Theoretical weight: 29.74 KDa
Source organism: Wolinella succinogenes
UniProt:
  • Canonical: P17413 (Residues: 1-256; Coverage: 100%)
Gene names: WS0832, frdC
Sequence domains: Succinate dehydrogenase/Fumarate reductase transmembrane subunit
Structure domains: Fumarate reductase/succinate dehydrogenase, transmembrane subunit

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD

Cofactor: Ligand HEM 4 x HEM
7 bound ligands:
Ligand CIT 2 x CIT
Ligand F3S 2 x F3S
Ligand NA 2 x NA
Ligand FES 2 x FES
Ligand SF4 2 x SF4
Ligand LMT 2 x LMT
Ligand DMW 2 x DMW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 85.104Å b: 188.766Å c: 117.817Å
α: 90° β: 104.47° γ: 90°
R-values:
R R work R free
0.2 0.2 0.216

Quick links

Citations

3 review citations

The quinone-binding and catalytic site of complex II.
Maklashina et al. (2010)
2 more

4 mentions without citation

Catalytic mechanisms of complex II enzymes: a structural perspective.
Iverson TM. (2013)
3 more