5t6m

Structure of the tryptophan synthase b-subunit from Pyroccus furiosus with b-methyltryptophan non-covalently boundStructure of the tryptophan synthase b-subunit from Pyroccus furiosus with b-methyltryptophan non-covalently bound

Structural highlights 5t6m is a 4 chain structure with sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: , , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRPB1_PYRFU The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine (By similarity). Publication Abstract from PubMed Tryptophan synthase (TrpS) catalyzes the final steps in the biosynthesis of l-tryptophan from l-serine (Ser) and indole-3-glycerol phosphate (IGP). We report that native TrpS can also catalyze a productive reaction with l-threonine (Thr), leading to (2S,3S)-beta-methyltryptophan. Surprisingly, beta-substitution occurs in vitro with a 3.4-fold higher catalytic efficiency for Ser over Thr using saturating indole, despite a >82000-fold preference for Ser in direct competition using IGP. Structural data identify a novel product binding site, and kinetic experiments clarify the atypical mechanism of specificity: Thr binds efficiently but decreases the affinity for indole and disrupts the allosteric signaling that regulates the catalytic cycle. Tryptophan Synthase Uses an Atypical Mechanism To Achieve Substrate Specificity.,Buller AR, van Roye P, Murciano-Calles J, Arnold FH Biochemistry. 2016 Dec 27;55(51):7043-7046. doi: 10.1021/acs.biochem.6b01127., Epub 2016 Dec 13. PMID:27935677 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tryptophan synthase 3D structures

spinqualitylabelsall models 5t6m, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image