Factors modulating conformational equilibria in large modular proteins: A case study with cobalamin-dependent methionine synthase
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference27 articles.
1. Activation of methionine synthase: Further characterization of the flavoprotein system
2. N5-Methyltetrahydrofolate-Homocysteine Transmethylase
3. Cloning and Sequence Analysis of the Escherichia coli metH Gene Encoding Cobalamin-dependent Methionine Synthase and Isolation of a Tryptic Fragment Containing the Cobalamin-binding Domain
4. Assignment of enzymic function to specific protein regions of cobalamin-dependent methionine synthase from Escherichia coli
5. Cobalamin-Dependent Methionine Synthase Is a Modular Protein with Distinct Regions for Binding Homocysteine, Methyltetrahydrofolate, Cobalamin, and Adenosylmethionine
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1. Theoretical study on the mechanism of tryptophan methylation catalyzed by the cobalamin-dependent radical enzyme TsrM;Journal of Catalysis;2024-01
2. Structure of full-length cobalamin-dependent methionine synthase and cofactor loading captured in crystallo;Nature Communications;2023-10-11
3. Conformational switching and flexibility in cobalamin-dependent methionine synthase studied by small-angle X-ray scattering and cryoelectron microscopy;Proceedings of the National Academy of Sciences;2023-06-20
4. Structure of full-length cobalamin-dependent methionine synthase and cofactor loading capturedin crystallo;2023-06-15
5. Conformational switching and flexibility in cobalamin-dependent methionine synthase studied by small-angle X-ray scattering and cryo-electron microscopy;2023-02-12
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