| http://purl.uniprot.org/citations/11967268 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11967268 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/11967268 | http://www.w3.org/2000/01/rdf-schema#comment | "The complex iron-sulfur flavoprotein glutamate synthase (GltS) plays a prominent role in ammonia assimilation in bacteria, yeasts, and plants. GltS catalyzes the formation of two molecules of l-glutamate from 2-oxoglutarate and l-glutamine via intramolecular channeling of ammonia. GltS has the impressive ability of synchronizing its distinct catalytic centers to avoid wasteful consumption of l-glutamine. We have determined the crystal structure of the ferredoxin-dependent GltS in several ligation and redox states. The structures reveal the crucial elements in the synchronization between the glutaminase site and the 2-iminoglutarate reduction site. The structural data combined with the catalytic properties of GltS indicate that binding of ferredoxin and 2-oxoglutarate to the FMN-binding domain of GltS induce a conformational change in the loop connecting the two catalytic centers. The rearrangement induces a shift in the catalytic elements of the amidotransferase domain, such that it becomes activated. This machinery, over a distance of more than 30 A, controls the ability of the enzyme to bind and hydrolyze the ammonia-donating substrate l-glutamine."xsd:string |
| http://purl.uniprot.org/citations/11967268 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m202541200"xsd:string |
| http://purl.uniprot.org/citations/11967268 | http://purl.uniprot.org/core/author | "Ferrari D."xsd:string |
| http://purl.uniprot.org/citations/11967268 | http://purl.uniprot.org/core/author | "Mattevi A."xsd:string |
| http://purl.uniprot.org/citations/11967268 | http://purl.uniprot.org/core/author | "van den Heuvel R.H."xsd:string |
| http://purl.uniprot.org/citations/11967268 | http://purl.uniprot.org/core/author | "Vanoni M.A."xsd:string |
| http://purl.uniprot.org/citations/11967268 | http://purl.uniprot.org/core/author | "Florencio F.J."xsd:string |
| http://purl.uniprot.org/citations/11967268 | http://purl.uniprot.org/core/author | "Curti B."xsd:string |
| http://purl.uniprot.org/citations/11967268 | http://purl.uniprot.org/core/author | "Bossi R.T."xsd:string |
| http://purl.uniprot.org/citations/11967268 | http://purl.uniprot.org/core/author | "Ravasio S."xsd:string |
| http://purl.uniprot.org/citations/11967268 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/11967268 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/11967268 | http://purl.uniprot.org/core/pages | "24579-24583"xsd:string |
| http://purl.uniprot.org/citations/11967268 | http://purl.uniprot.org/core/title | "Structural studies on the synchronization of catalytic centers in glutamate synthase."xsd:string |
| http://purl.uniprot.org/citations/11967268 | http://purl.uniprot.org/core/volume | "277"xsd:string |
| http://purl.uniprot.org/citations/11967268 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11967268 |
| http://purl.uniprot.org/citations/11967268 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11967268 |
| http://purl.uniprot.org/citations/11967268 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11967268 |
| http://purl.uniprot.org/citations/11967268 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11967268 |
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| http://purl.uniprot.org/uniprot/P55038 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11967268 |