Entry | Database: PDB / ID: 8ssc |
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Title | Full-Length Methionine synthase from Thermus thermophilus HB8 |
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Components | Methionine synthase |
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Keywords | TRANSFERASE / Methyl transferase / cobalamin-dependent / cobalamin binding / one-carbon metabolism |
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Function / homology | Function and homology information
methionine synthase / methionine synthase activity / homocysteine metabolic process / cobalamin binding / tetrahydrofolate metabolic process / methylation / zinc ion binding / cytosolSimilarity search - Function Vitamin B12-dependent methionine synthase, activation domain / Vitamin B12 dependent methionine synthase, activation domain / AdoMet activation domain profile. / Cobalamin-dependent methionine synthase / Methionine synthase, B12-binding domain / Vitamin B12-dependent methionine synthase, activation domain superfamily / B12-binding N-terminal domain profile. / B12 binding domain / Homocysteine-binding domain / Homocysteine-binding domain superfamily ...Vitamin B12-dependent methionine synthase, activation domain / Vitamin B12 dependent methionine synthase, activation domain / AdoMet activation domain profile. / Cobalamin-dependent methionine synthase / Methionine synthase, B12-binding domain / Vitamin B12-dependent methionine synthase, activation domain superfamily / B12-binding N-terminal domain profile. / B12 binding domain / Homocysteine-binding domain / Homocysteine-binding domain superfamily / Homocysteine S-methyltransferase / Homocysteine-binding domain profile. / Cobalamin (vitamin B12)-binding module, cap domain / B12 binding domain / Methionine synthase domain / B12 binding domain / Cobalamin-binding domain superfamily / B12-binding domain profile. / Cobalamin (vitamin B12)-binding domain / Pterin-binding domain / Pterin binding enzyme / Pterin-binding domain profile. / Dihydropteroate synthase-likeSimilarity search - Domain/homology |
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Biological species | Thermus thermophilus HB8 (bacteria) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.75 Å |
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Authors | Yamada, K. / Mendoza, J. / Koutmos, M. |
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Funding support | United States, 1items Organization | Grant number | Country |
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National Science Foundation (NSF, United States) | 1945174 | United States |
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Citation | Journal: Nat Commun / Year: 2023 Title: Structure of full-length cobalamin-dependent methionine synthase and cofactor loading captured in crystallo. Authors: Mendoza, J. / Purchal, M. / Yamada, K. / Koutmos, M. |
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History | Deposition | May 8, 2023 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Oct 18, 2023 | Provider: repository / Type: Initial release |
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Revision 1.1 | Oct 25, 2023 | Group: Database references / Category: citation / citation_author Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name |
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