1ofd: Difference between revisions
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Revision as of 16:47, 30 October 2007
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GLUTAMATE SYNTHASE FROM SYNECHOCYSTIS SP IN COMPLEX WITH 2-OXOGLUTARATE AT 2.0 ANGSTROM RESOLUTION
OverviewOverview
Glutamate synthases (GltS) are crucial enzymes in ammonia assimilation in, plants and bacteria, where they catalyze the formation of two molecules of, L-glutamate from L-glutamine and 2-oxoglutarate. The plant-type, ferredoxin-dependent GltS and the functionally homologous alpha subunit of, the bacterial NADPH-dependent GltS are complex four-domain monomeric, enzymes of 140-165 kDa belonging to the NH(2)-terminal nucleophile family, of amidotransferases. The enzymes function through the channeling of, ammonia from the N-terminal amidotransferase domain to the FMN-binding, domain. Here, we report the X-ray structure of the Synechocystis, ferredoxin-dependent GltS with the substrate 2-oxoglutarate and the, covalent inhibitor 5-oxo-L-norleucine bound in their physically distinct, active ... [(full description)]
About this StructureAbout this Structure
1OFD is a [Single protein] structure of sequence from [Synechocystis sp.] with FMN, F3S and AKG as [ligands]. Active as [Glutamate synthase (ferredoxin)], with EC number [1.4.7.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
The active conformation of glutamate synthase and its binding to ferredoxin., van den Heuvel RH, Svergun DI, Petoukhov MV, Coda A, Curti B, Ravasio S, Vanoni MA, Mattevi A, J Mol Biol. 2003 Jun 27;330(1):113-28. PMID:12818206
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