| http://purl.uniprot.org/citations/20375021 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20375021 | http://www.w3.org/2000/01/rdf-schema#comment | "Aminomethyltransferase, a component of the glycine cleavage system termed T-protein, reversibly catalyzes the degradation of the aminomethyl moiety of glycine attached to the lipoate cofactor of H-protein, resulting in the production of ammonia, 5,10-methylenetetrahydrofolate, and dihydrolipoate-bearing H-protein in the presence of tetrahydrofolate. Several mutations in the human T-protein gene are known to cause nonketotic hyperglycinemia. Here, we report the crystal structure of Escherichia coli T-protein in complex with dihydrolipoate-bearing H-protein and 5-methyltetrahydrofolate, a complex mimicking the ternary complex in the reverse reaction. The structure of the complex shows a highly interacting intermolecular interface limited to a small area and the protein-bound dihydrolipoyllysine arm inserted into the active site cavity of the T-protein. Invariant Arg(292) of the T-protein is essential for complex assembly. The structure also provides novel insights in understanding the disease-causing mutations, in addition to the disease-related impairment in the cofactor-enzyme interactions reported previously. Furthermore, structural and mutational analyses suggest that the reversible transfer of the methylene group between the lipoate and tetrahydrofolate should proceed through the electron relay-assisted iminium intermediate formation."xsd:string |
| http://purl.uniprot.org/citations/20375021 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.110718"xsd:string |
| http://purl.uniprot.org/citations/20375021 | http://purl.uniprot.org/core/author | "Fujiwara K."xsd:string |
| http://purl.uniprot.org/citations/20375021 | http://purl.uniprot.org/core/author | "Nakagawa A."xsd:string |
| http://purl.uniprot.org/citations/20375021 | http://purl.uniprot.org/core/author | "Taniguchi H."xsd:string |
| http://purl.uniprot.org/citations/20375021 | http://purl.uniprot.org/core/author | "Maita N."xsd:string |
| http://purl.uniprot.org/citations/20375021 | http://purl.uniprot.org/core/author | "Okamura-Ikeda K."xsd:string |
| http://purl.uniprot.org/citations/20375021 | http://purl.uniprot.org/core/author | "Hosaka H."xsd:string |
| http://purl.uniprot.org/citations/20375021 | http://purl.uniprot.org/core/author | "Yoshizawa A.C."xsd:string |
| http://purl.uniprot.org/citations/20375021 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20375021 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/20375021 | http://purl.uniprot.org/core/pages | "18684-18692"xsd:string |
| http://purl.uniprot.org/citations/20375021 | http://purl.uniprot.org/core/title | "Crystal structure of aminomethyltransferase in complex with dihydrolipoyl-H-protein of the glycine cleavage system: implications for recognition of lipoyl protein substrate, disease-related mutations, and reaction mechanism."xsd:string |
| http://purl.uniprot.org/citations/20375021 | http://purl.uniprot.org/core/volume | "285"xsd:string |
| http://purl.uniprot.org/citations/20375021 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20375021 |
| http://purl.uniprot.org/citations/20375021 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20375021 |
| http://purl.uniprot.org/uniprot/#_P27248-mappedCitation-20375021 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/20375021 |
| http://purl.uniprot.org/uniprot/#_P0A6T9-mappedCitation-20375021 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/20375021 |
| http://purl.uniprot.org/uniprot/P27248 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/20375021 |
| http://purl.uniprot.org/uniprot/P0A6T9 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/20375021 |