Crystallization (Comment) | Organism |
---|---|
crystal structure of QFR to 3.3 A resolution. Enzyme contains two quinone species, presumably menaquinol, bound to the transmembrane-spanning region. The binding sites for the two quinone molecules are termed QP and QD, indicating their positions proximal, QP, or distal, QD, to the site of fumarate reduction in the hydrophilic flavoprotein and iron-sulfur protein subunits. Co-crystallization studies of the Escherichia coli QFR with the quinol-binding site inhibitors 2-heptyl-4-hydroxyquinoline-N-oxide and 2-[1-(p-chlorophenyl)ethyl] 4,6-dinitrophenol establish that both inhibitors block the binding of MQH2 at the QP site. In the structures with the inhibitor bound at QP, no density is observed at QD. The conserved acidic residue, Glu29 in subunit FrdC, in the Escherichia coli enzyme may act as a proton shuttle from the quinol during enzyme turnover | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-heptyl-4-hydroxyquinoline N-oxide | inhibitor blocks the binding of menaquinol at the proximal quinone binding-site, crystallization studies | Escherichia coli | |
2-[1-(p-chlorophenyl)ethyl] 4,6-dinitrophenol | inhibitor blocks the binding of menaquinol at the proximal quinone binding-site, crystallization studies | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Escherichia coli | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P00363 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
QFR | - |
Escherichia coli |