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Structure paper

TitleStructure of active IspH enzyme from Escherichia coli provides mechanistic insights into substrate reduction.
Journal, issue, pagesAngew. Chem. Int. Ed. Engl., Vol. 48, Page 5756-5759, Year 2009
Publish dateNov 10, 2008 (structure data deposition date)
AuthorsGrawert, T. / Rohdich, F. / Span, I. / Bacher, A. / Eisenreich, W. / Eppinger, J. / Groll, M.
External linksAngew. Chem. Int. Ed. Engl. / PubMed:19569147
MethodsX-ray diffraction
Resolution1.8 Å
Structure data

PDB-3f7t:
Structure of active IspH shows a novel fold with a [3Fe-4S] cluster in the catalytic centre
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-F3S:
FE3-S4 CLUSTER

ChemComp-POP:
PYROPHOSPHATE 2-

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsOXIDOREDUCTASE / pseudo-C3-symmetry; unprecedent fold for FeS-cluster proteins / Iron / Iron-sulfur / Isoprene biosynthesis / Metal-binding / NADP / PROTEIN BINDING

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