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A disulfide-stabilized conformer of methionine synthase reveals an unexpected role for the histidine ligand of the cobalamin cofactor
B(12)-dependent methionine synthase (MetH) from Escherichia coli is a large modular protein that is alternately methylated by methyltetrahydrofolate to form methylcobalamin and demethylated by homocysteine to form cob(I)alamin. Major domain rearrangements are required to allow cobalamin to react wit...
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| Autori principali: | , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
2008
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2393809/ https://ncbi.nlm.nih.gov/pubmed/18332423 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0800329105 |
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