1qoq: Difference between revisions
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[[Category: tryptophan biosynthesis]] | [[Category: tryptophan biosynthesis]] | ||
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CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH INDOLE GLYCEROL PHOSPHATE
OverviewOverview
We used freeze trapping to stabilize the Michaelis complex of wild-type, tryptophan synthase and the alpha-subunit substrate indole-3-glycerol, phosphate (IGP) and determined its structure to 1. 8 A resolution. In, addition, we determined the 1.4 A resolution structure of the complex with, indole-3-propanole phosphate (IPP), a noncleavable IGP analogue. The, interaction of the 3'-hydroxyl of IGP with the catalytic alphaGlu49 leads, to a twisting of the propane chain and to a repositioning of the indole, ring compared to IPP. Concomitantly, the catalytic alphaAsp60 rotates, resulting in a translocation of the COMM domain [betaGly102-betaGly189, for definition see Schneider et al. (1998) Biochemistry 37, 5394-5406] in, a direction opposite to the one in the IPP complex. This results in ... [(full description)]
About this StructureAbout this Structure
1QOQ is a [Protein complex] structure of sequences from [Salmonella typhimurium] with IGP and PLP as [ligands]. Active as [Tryptophan synthase], with EC number [4.2.1.20]. Structure known Active Site: IGP. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of wild-type tryptophan synthase complexed with the natural substrate indole-3-glycerol phosphate., Weyand M, Schlichting I, Biochemistry. 1999 Dec 14;38(50):16469-80. PMID:10600108
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