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TitleStructural basis of S-adenosylmethionine-dependent allosteric transition from active to inactive states in methylenetetrahydrofolate reductase.
Journal, issue, pagesNat Commun, Vol. 15, Page 5167-5167, Year 2024
Publish dateNov 12, 2023 (structure data deposition date)
AuthorsYamada, K. / Mendoza, J. / Koutmos, M.
External linksNat Commun / PubMed:38886362
MethodsX-ray diffraction
Resolution2.83 - 3.49 Å
Structure data

PDB-8uy1:
Methylenetetrahydrofolate reductase from Chaetomium thermophilum DSM 1495, Active (R) State
Method: X-RAY DIFFRACTION / Resolution: 3.49 Å

PDB-8uy2:
Methylenetetrahydrofolate reductase from Chaetomium thermophilum DSM 1495, AdoMet-bound, Inhibited (T) State
Method: X-RAY DIFFRACTION / Resolution: 2.83 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-HOH:
WATER

ChemComp-SAM:
S-ADENOSYLMETHIONINE

ChemComp-ACT:
ACETATE ION

ChemComp-SO4:
SULFATE ION

ChemComp-NA:
Unknown entry

ChemComp-GOL:
GLYCEROL

Source
  • thermochaetoides thermophila dsm 1495 (fungus)
KeywordsOXIDOREDUCTASE / methylenetetrahydrofolate reductase / NADPH activity / oxidoreductase activity / acting on the CH-NH group of donors / NAD or NADP as acceptor cobalamin binding / one-carbon metabolism / OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR / OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex

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