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TitleWater-Mediated Carbon-Oxygen Hydrogen Bonding Facilitates S-Adenosylmethionine Recognition in the Reactivation Domain of Cobalamin-Dependent Methionine Synthase.
Journal, issue, pagesBiochemistry, Vol. 57, Page 3733-3740, Year 2018
Publish dateOct 24, 2017 (structure data deposition date)
AuthorsFick, R.J. / Clay, M.C. / Vander Lee, L. / Scheiner, S. / Al-Hashimi, H. / Trievel, R.C.
External linksBiochemistry / PubMed:29733595
MethodsX-ray diffraction
Resolution1.5 - 1.512 Å
Structure data

PDB-6bdy:
Crystal Structure of the MetH Reactivation Domain bound to Sinefungin
Method: X-RAY DIFFRACTION / Resolution: 1.512 Å

PDB-6bm5:
Crystal Structure of the MetH Reactivation Domain bound to AdoMet
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-6bm6:
Crystal Structure of the MetH Reactivation Domain bound to AdoHcy
Method: X-RAY DIFFRACTION / Resolution: 1.504 Å

Chemicals

ChemComp-SFG:
SINEFUNGIN

ChemComp-HOH:
WATER

ChemComp-SAM:
S-ADENOSYLMETHIONINE

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / C-terminal domain / reactivation domain / MetH-sinefungin / TRANSFERASE / TRANSFERASE-TRANSFERASE INHIBITOR complex / MetH-AdoMet / MetH-SAM / MetH-AdoHcy / MetH-SAH

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