Conformational switching and flexibility in cobalamin-dependent methionine synthase studied by small-angle X-ray scattering and cryoelectron microscopy.
Enzyme dynamics
SAXS
cryo-EM
one-carbon metabolism
structure prediction
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
27 06 2023
27 06 2023
Historique:
medline:
22
6
2023
pubmed:
20
6
2023
entrez:
20
6
2023
Statut:
ppublish
Résumé
Cobalamin-dependent methionine synthase (MetH) catalyzes the synthesis of methionine from homocysteine and 5-methyltetrahydrofolate (CH
Identifiants
pubmed: 37339208
doi: 10.1073/pnas.2302531120
pmc: PMC10293825
doi:
Substances chimiques
5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase
EC 2.1.1.13
Methionine
AE28F7PNPL
Folic Acid
935E97BOY8
Vitamin B 12
P6YC3EG204
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2302531120Subventions
Organisme : NIGMS NIH HHS
ID : P30 GM124166
Pays : United States
Organisme : NIGMS NIH HHS
ID : R00 GM100008
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM124847
Pays : United States
Organisme : NIH HHS
ID : S10 OD028617
Pays : United States
Organisme : NIGMS NIH HHS
ID : U24 GM129539
Pays : United States
Organisme : NIGMS NIH HHS
ID : K99 GM100008
Pays : United States
Commentaires et corrections
Type : UpdateOf
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