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TitleNew crystal forms of the integral membrane Escherichia coli quinol:fumarate reductase suggest that ligands control domain movement.
Journal, issue, pagesJ. Struct. Biol., Vol. 202, Page 100-104, Year 2018
Publish dateSep 5, 2017 (structure data deposition date)
AuthorsStarbird, C.A. / Tomasiak, T.M. / Singh, P.K. / Yankovskaya, V. / Maklashina, E. / Eisenbach, M. / Cecchini, G. / Iverson, T.M.
External linksJ. Struct. Biol. / PubMed:29158068
MethodsX-ray diffraction
Resolution3.35 Å
Structure data

PDB-6awf:
Escherichia coli quinol:fumarate reductase crystallized without dicarboxylate
Method: X-RAY DIFFRACTION / Resolution: 3.35 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-PO4:
PHOSPHATE ION

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-F3S:
FE3-S4 CLUSTER

ChemComp-SF4:
IRON/SULFUR CLUSTER

Source
  • escherichia coli (E. coli)
KeywordsELECTRON TRANSPORT / Complex II / quinol:fumarate reductase / fumarate reductase / succinate dehydrogenase / succinate oxidase / succinate:quinone oxidoreductase / FAD / flavoprotein / flavoenzyme

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