2cll

File:2cll.gif

spinqualitylabelsall models 2cll, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

TRYPTOPHAN SYNTHASE (EXTERNAL ALDIMINE STATE) IN COMPLEX WITH N-(4'-TRIFLUOROMETHOXYBENZENESULFONYL)-2-AMINO-1-ETHYLPHOSPHATE (F9)

OverviewOverview

Allosteric interactions regulate substrate channeling in Salmonella, typhimurium tryptophan synthase. The channeling of indole between the, alpha- and beta-sites via the interconnecting 25 A tunnel is regulated by, allosteric signaling arising from binding of ligand to the alpha-site, and, covalent reaction of l-Ser at the beta-site. This signaling switches the, alpha- and beta-subunits between open conformations of low activity and, closed conformations of high activity. Our objective is to synthesize and, characterize new classes of alpha-site ligands (ASLs) that mimic the, binding of substrates, 3-indole-d-glycerol 3'-phosphate (IGP) or, d-glyceraldehyde 3-phosphate (G3P), for use in the investigation of, alpha-site-beta-site interactions. The new synthesized IGP analogues, contain an ... [(full description)]

About this StructureAbout this Structure

2CLL is a [Protein complex] structure of sequences from [Salmonella typhimurium] with NA, F9F and PLS as [ligands]. Active as [Tryptophan synthase], with EC number [4.2.1.20]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

Synthesis and characterization of allosteric probes of substrate channeling in the tryptophan synthase bienzyme complex., Ngo H, Harris R, Kimmich N, Casino P, Niks D, Blumenstein L, Barends TR, Kulik V, Weyand M, Schlichting I, Dunn MF, Biochemistry. 2007 Jul 3;46(26):7713-27. Epub 2007 Jun 9. PMID:17559195

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