2cli
TRYPTOPHAN SYNTHASE IN COMPLEX WITH N-(4'-TRIFLUOROMETHOXYBENZENESULFONYL)-2-AMINO-1-ETHYLPHOSPHATE (F9)
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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
2CLI is a [Protein complex] structure of sequences from [Salmonella typhimurium] with NA, F9F and PLP 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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