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Structure paper

TitleStructural basis for glycyl radical formation by pyruvate formate-lyase activating enzyme.
Journal, issue, pagesProc. Natl. Acad. Sci. Usa, Vol. 105, Page 16137-16141, Year 2008
Publish dateFeb 11, 2008 (structure data deposition date)
AuthorsVey, J.L. / Yang, J. / Li, M. / Broderick, W.E. / Broderick, J.B. / Drennan, C.L.
External linksProc. Natl. Acad. Sci. Usa / PubMed:18852451
MethodsX-ray diffraction
Resolution2.25 - 2.77 Å
Structure data

PDB-3c8f:
4Fe-4S-Pyruvate formate-lyase Activating Enzyme with partially disordered AdoMet
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-3cb8:
4Fe-4S-Pyruvate formate-lyase activating enzyme in complex with AdoMet and a peptide substrate
Method: X-RAY DIFFRACTION / Resolution: 2.77 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-MT2:
[(3S)-3-amino-3-carboxypropyl](ethyl)methylsulfonium

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-SAM:
S-ADENOSYLMETHIONINE

ChemComp-FMT:
FORMIC ACID

Source
  • escherichia coli (E. coli)
KeywordsOXIDOREDUCTASE / AdoMet radical / SAM radical / activase / glycyl radical / Carbohydrate metabolism / Glucose metabolism / Iron / Iron-sulfur / Metal-binding / S-adenosyl-L-methionine / partial TIM barrel / 4Fe-4S / Cytoplasm

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