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TitleInsights into the reactivation of cobalamin-dependent methionine synthase.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 106, Page 18527-18532, Year 2009
Publish dateAug 31, 2009 (structure data deposition date)
AuthorsKoutmos, M. / Datta, S. / Pattridge, K.A. / Smith, J.L. / Matthews, R.G.
External linksProc. Natl. Acad. Sci. USA / PubMed:19846791
MethodsX-ray diffraction
Resolution2.7 - 3.25 Å
Structure data

PDB-3iv9:
Structure of the B12-dependent Methionine Synthase (MetH) C-teminal half in a "His-On" conformation
Method: X-RAY DIFFRACTION / Resolution: 3.25 Å

PDB-3iva:
Structure of the B12-dependent Methionine Synthase (MetH) C-teminal half with AdoHcy bound
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-B12:
COBALAMIN

ChemComp-HOH:
WATER

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-NO3:
NITRATE ION

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / METH / reactivation conformation / H759 / cobalamin / intermodular interactions / amino-acid biosynthesis / cobalt / metal-binding / methionine biosynthesis / methyltransferase / S-adenosyl-L-methionine / S-adenosyl-homocysteine

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