ArticleNature communications2023
Structure of full-length cobalamin-dependent methionine synthase and cofactor loading captured in crystallo.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Recovery of a minor cryo-EM particle population reveals conformational equilibria linking cofactor loading, turnover, and reactivation in methionine synthase.bioRxiv : the preprint server for biology · 2026Article
- Sulfur-Containing Amino Acids: The Conversion Process from Product to Substrate.International journal of molecular sciences · 2026Review
- Structural insights into cobalamin loading and reactivation of human methionine synthase.Nature communications · 2026Article
- Monitoring the Switching from Base-on to Base-off Forms of Vitamin BAnalytical chemistry · 2026Article
- The therapeutic potential of vitamins as nutrients in food for anti-inflammatory and anti-oxidative stress in liver fibrosis diseases.Frontiers in nutrition · 2026Review
- Laboratory evolution ofJournal of bacteriology · 2025Article
- Corrinoid salvaging and cobamide remodeling in bacteria and archaea.Journal of bacteriology · 2024Review
- Laboratory evolution ofbioRxiv : the preprint server for biology · 2024Article
- Emerging Roles of Vitamin BInternational journal of molecular sciences · 2024Review
- Synergistic Differential DNA Demethylation Activity ofBiomedicines · 2024Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cobalamin-dependent methionine synthase (MS) is a key enzyme in methionine and folate one-carbon metabolism. MS is a large multi-domain protein capable of binding and activating three substrates: homocysteine, folate, and S-adenosylmethionine for methylation. Achieving three chemically distinct methylations necessitates significant domain rearrangements to facilitate substrate access to the cobalamin cofactor at the right time. The distinct conformations required for each reaction have eluded structural characterization as its inherently dynamic nature renders structural studies difficult. Here, we use a thermophilic MS homolog (tMS) as a functional MS model. Its exceptional stability enabled characterization of MS in the absence of cobalamin, marking the only studies of a cobalamin-binding protein in its apoenzyme state. More importantly, we report the high-resolution full-length MS structure, ending a multi-decade quest. We also capture cobalamin loading in crystallo, providing structural insights into holoenzyme formation. Our work paves the way for unraveling how MS orchestrates large-scale domain rearrangements crucial for achieving challenging chemistries.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.