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Structure paper

TitleClosed fumarase C active-site structures reveal SS Loop residue contribution in catalysis.
Journal, issue, pagesFebs Lett., Vol. 594, Page 337-357, Year 2020
Publish dateFeb 13, 2019 (structure data deposition date)
AuthorsStuttgen, G.M. / Grosskopf, J.D. / Berger, C.R. / May, J.F. / Bhattacharyya, B. / Weaver, T.M.
External linksFebs Lett. / PubMed:31514245
MethodsX-ray diffraction
Resolution1.37 - 1.528 Å
Structure data

PDB-6nz9:
Crystal structure of E. coli fumarase C bound to citrate at 1.53 angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 1.528 Å

PDB-6nza:
Crystal structure of E. coli fumarase C K324A variant with closed SS Loop at 1.41 angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 1.406 Å

PDB-6nzb:
Crystal structure of E. coli fumarase C S318A variant with closed SS Loop at 1.37 angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 1.37 Å

PDB-6nzc:
Crystal structure of E. coli fumarase C N326A variant with closed SS Loop at 1.40 angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 1.403 Å

Chemicals

ChemComp-CIT:
CITRIC ACID

ChemComp-HOH:
WATER

Source
  • escherichia coli (strain k12) (bacteria)
KeywordsLYASE / fumarase / inhibitor complex / metabolism / Krebs Cycle / citrate

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