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1a5s
From Proteopedia
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[[Category: tryptophan biosynthesis]] | [[Category: tryptophan biosynthesis]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:45:26 2007'' |
Revision as of 12:40, 30 October 2007
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CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUOROINDOLE PROPANOL PHOSPHATE AND L-SER BOUND AS AMINO ACRYLATE TO THE BETA SITE
Overview
Crystal structures of wild-type tryptophan synthase alpha2beta2 complexes, from Salmonella typhimurium were determined to investigate the mechanism, of allosteric activation of the alpha-reaction by the aminoacrylate, intermediate formed at the beta-active site. Using a flow cell, the, aminoacrylate (A-A) intermediate of the beta-reaction () was generated in, the crystal under steady state conditions in the presence of serine and, the alpha-site inhibitor 5-fluoroindole propanol phosphate (F-IPP). A, model for the conformation of the Schiff base between the aminoacrylate, and the beta-subunit cofactor pyridoxal phosphate (PLP) is presented. The, structure is compared with structures of the enzyme determined in the, absence (TRPS) and presence (TRPSF-IPP) of F-IPP. A detailed model for, ... [(full description)]
About this Structure
1A5S is a [Protein complex] structure of sequences from [Salmonella typhimurium] with NA, FIP, PLP and SER as [ligands]. Active as [Tryptophan synthase], with EC number [4.2.1.20]. Structure known Active Sites: S1 and S2. Full crystallographic information is available from [OCA].
Reference
Loop closure and intersubunit communication in tryptophan synthase., Schneider TR, Gerhardt E, Lee M, Liang PH, Anderson KS, Schlichting I, Biochemistry. 1998 Apr 21;37(16):5394-406. PMID:9548921
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