This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1qoq
From Proteopedia
|
CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH INDOLE GLYCEROL PHOSPHATE
Overview
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 Structure
1QOQ is a [Protein complex] structure of sequences from [Salmonella typhimurium] with IGP and PLP as [ligands]. Active as [Lyase], with EC number [4.2.1.20]. Structure known Active Site: IGP. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Tue Oct 30 08:36:27 2007
