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Structure paper

TitleX-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 110, Page 8519-8524, Year 2013
Publish dateApr 10, 2013 (structure data deposition date)
AuthorsGoldman, P.J. / Grove, T.L. / Sites, L.A. / McLaughlin, M.I. / Booker, S.J. / Drennan, C.L.
External linksProc. Natl. Acad. Sci. USA / PubMed:23650368
MethodsX-ray diffraction
Resolution1.619 - 1.831 Å
Structure data

PDB-4k36:
His6 tagged anSMEcpe with bound AdoMet
Method: X-RAY DIFFRACTION / Resolution: 1.619 Å

PDB-4k37:
Native anSMEcpe with bound AdoMet
Method: X-RAY DIFFRACTION / Resolution: 1.62 Å

PDB-4k38:
Native anSMEcpe with bound AdoMet and Kp18Cys peptide
Method: X-RAY DIFFRACTION / Resolution: 1.831 Å

PDB-4k39:
Native anSMEcpe with bound AdoMet and Cp18Cys peptide
Method: X-RAY DIFFRACTION / Resolution: 1.783 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-SAM:
S-ADENOSYLMETHIONINE

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

Source
  • clostridium perfringens (bacteria)
KeywordsOXIDOREDUCTASE / AdoMet radical fold

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