2tsy

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2tsy, resolution 2.5Å

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CRYSTAL STRUCTURES OF MUTANT (BETAK87T) TRYPTOPHAN SYNTHASE ALPHA2 BETA2 COMPLEX WITH LIGANDS BOUND TO THE ACTIVE SITES OF THE ALPHA AND BETA SUBUNITS REVEAL LIGAND-INDUCED CONFORMATIONAL CHANGES

Overview

Three-dimensional structures are reported for a mutant (betaK87T), tryptophan synthase alpha2beta2 complex with either the substrate L-serine, (betaK87T-Ser) or product L-tryptophan (betaK87T-Trp) at the active site, of the beta-subunit, in which both amino acids form external aldimines, with the coenzyme, pyridoxal phosphate. We also present structures with, L-serine bound to the beta site and either alpha-glycerol 3-phosphate, (betaK87T-Ser-GP) or indole-3-propanol phosphate (betaK87T-Ser-IPP) bound, to the active site of the alpha-subunit. The results further identify the, substrate and product binding sites in each subunit and provide insight, into conformational changes that occur upon formation of these complexes., The two structures having ligands at the active sites of both alpha- ... [(full description)]

About this Structure

2TSY is a [Protein complex] structure of sequences from [Salmonella typhimurium] with NA, G3P and PLS as [ligands]. Active as [[1]], with EC number [4.2.1.20]. Full crystallographic information is available from [OCA].

Reference

Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes., Rhee S, Parris KD, Hyde CC, Ahmed SA, Miles EW, Davies DR, Biochemistry. 1997 Jun 24;36(25):7664-80. PMID:9201907

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