1ofd
From Proteopedia
|
GLUTAMATE SYNTHASE FROM SYNECHOCYSTIS SP IN COMPLEX WITH 2-OXOGLUTARATE AT 2.0 ANGSTROM RESOLUTION
Overview
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 Structure
1OFD is a [Single protein] structure of sequence from [Synechocystis sp.] with FMN, F3S and AKG as [ligands]. Active as [[1]], with EC number [1.4.7.1]. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Mon Oct 29 19:52:43 2007
Categories: Single protein | Synechocystis sp. | Heuvel, R.H.H.Van.Den. | Mattevi, A. | AKG | F3S | FMN | Amidotransferase | Complex enzyme | Fad | Fd-gogat | Flavoprotein | Fmn | Iron-sulphur | Oxidoreductase | Substrate channeling