› 6awf

X-ray diffraction
3.35Å resolution

Escherichia coli quinol:fumarate reductase crystallized without dicarboxylate

Released:
DOI: 10.2210/pdb6awf/pdb
PDB entry 6awf coloured by chain, front view.
PDB entry 6awf coloured by chain, side view.
PDB entry 6awf coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
New crystal forms of the integral membrane Escherichia coli quinol:fumarate reductase suggest that ligands control domain movement.
Starbird CA, Tomasiak TM, Singh PK, Yankovskaya V, Maklashina E, Eisenbach M, Cecchini G, Iverson TM
J Struct Biol 202 100-104 (2018)
PMID: 29158068

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132435 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Fumarate reductase flavoprotein subunit Chains: A, E
Molecule details ›
Chains: A, E
Length: 602 amino acids
Theoretical weight: 66.06 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00363 (Residues: 1-602; Coverage: 100%)
Gene names: JW4115, b4154, frdA
Sequence domains:
Structure domains:
Fumarate reductase iron-sulfur subunit Chains: B, F
Molecule details ›
Chains: B, F
Length: 243 amino acids
Theoretical weight: 27.02 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AC47 (Residues: 2-244; Coverage: 100%)
Gene names: JW4114, b4153, frdB
Sequence domains:
Structure domains:
Fumarate reductase subunit C Chains: C, G
Molecule details ›
Chains: C, G
Length: 130 amino acids
Theoretical weight: 14.9 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A8Q0 (Residues: 2-131; Coverage: 99%)
Gene names: JW4113, b4152, frdC
Sequence domains: Fumarate reductase subunit C
Structure domains: Fumarate reductase/succinate dehydrogenase, transmembrane subunit
Fumarate reductase subunit D Chains: D, H
Molecule details ›
Chains: D, H
Length: 119 amino acids
Theoretical weight: 13.12 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A8Q3 (Residues: 1-119; Coverage: 100%)
Gene names: JW4112, b4151, frdD
Sequence domains: Fumarate reductase subunit D
Structure domains: Fumarate reductase/succinate dehydrogenase, transmembrane subunit

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
4 bound ligands:
Ligand PO4 2 x PO4
Ligand FES 2 x FES
Ligand F3S 2 x F3S
Ligand SF4 2 x SF4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P21
Unit cell:
a: 113.318Å b: 117.986Å c: 125.291Å
α: 90° β: 98.8° γ: 90°
R-values:
R R work R free
0.286 0.285 0.318
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

The unassembled flavoprotein subunits of human and bacterial complex II have impaired catalytic activity and generate only minor amounts of ROS.
Maklashina et al. (2018)
4 more

2 mentions without citation

Inducible intracellular membranes: molecular aspects and emerging applications.
Royes et al. (2020)
1 more