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spinqualitylabelsall models 1ofe, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

GLUTAMATE SYNTHASE FROM SYNECHOCYSTIS SP IN COMPLEX WITH 2-OXOGLUTARATE AND L-DON AT 2.45 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

1OFE is a [Single protein] structure of sequence from [Synechocystis sp.] with F3S, FMN, AKG and ONL 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

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