| http://purl.uniprot.org/citations/11731805 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11731805 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11731805 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/11731805 | http://www.w3.org/2000/01/rdf-schema#comment | "B(12)-dependent methionine synthase (MetH) from Escherichia coli is a large modular protein that uses bound cobalamin as an intermediate methyl carrier. Major domain rearrangements have been postulated to explain how cobalamin reacts with three different substrates: homocysteine, methyltetrahydrofolate and S-adenosylmethionine (AdoMet). Here we describe the 3.0 A structure of a 65 kDa C-terminal fragment of MetH that spans the cobalamin- and AdoMet-binding domains, arranged in a conformation suitable for the methyl transfer from AdoMet to cobalamin that occurs during activation. In the conversion to the activation conformation, a helical domain that capped the cofactor moves 26 A and rotates by 63 degrees, allowing formation of a new interface between cobalamin and the AdoMet-binding (activation) domain. Interactions with the MetH activation domain drive the cobalamin away from its binding domain in a way that requires dissociation of the axial cobalt ligand and, thereby, provide a mechanism for control of the distribution of enzyme conformations."xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.org/dc/terms/identifier | "doi:10.1038/nsb738"xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.org/dc/terms/identifier | "doi:10.1038/nsb738"xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/author | "Bandarian V."xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/author | "Bandarian V."xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/author | "Ludwig M.L."xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/author | "Ludwig M.L."xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/author | "Matthews R.G."xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/author | "Matthews R.G."xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/author | "Huddler D.P."xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/author | "Huddler D.P."xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/author | "Pattridge K.A."xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/author | "Pattridge K.A."xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/author | "Lennon B.W."xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/author | "Lennon B.W."xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/name | "Nat. Struct. Biol."xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/name | "Nat. Struct. Biol."xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/pages | "53-56"xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/pages | "53-56"xsd:string |
| http://purl.uniprot.org/citations/11731805 | http://purl.uniprot.org/core/title | "Domain alternation switches B(12)-dependent methionine synthase to the activation conformation."xsd:string |