1a50
From Proteopedia
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CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUOROINDOLE PROPANOL PHOSPHATE
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
1A50 is a [Protein complex] structure of sequences from [Salmonella typhimurium] with NA, PLP and FIP as [ligands]. Active as [[1]], with EC number [4.2.1.20]. 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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