5e0k

X-ray crystal structure of tryptophan synthase complex from Pyrococcus furiosus at 2.76 A

spinqualitylabelsall models 5e0k, resolution 2.76Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5e0k is a 12 chain structure with sequence from Pyrfu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4 NonStd Res: LLP Related: 5dvz, 5dw0, 5dw3 Gene: trpA, PF1705 (PYRFU), trpB1, PF1706 (PYRFU) Activity: Tryptophan synthase, with EC number 4.2.1.20 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TRPA_PYRFU] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [TRPB1_PYRFU] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine (By similarity). Publication Abstract from PubMed Enzymes in heteromeric, allosterically regulated complexes catalyze a rich array of chemical reactions. Separating the subunits of such complexes, however, often severely attenuates their catalytic activities, because they can no longer be activated by their protein partners. We used directed evolution to explore allosteric regulation as a source of latent catalytic potential using the beta-subunit of tryptophan synthase from Pyrococcus furiosus (PfTrpB). As part of its native alphabetabetaalpha complex, TrpB efficiently produces tryptophan and tryptophan analogs; activity drops considerably when it is used as a stand-alone catalyst without the alpha-subunit. Kinetic, spectroscopic, and X-ray crystallographic data show that this lost activity can be recovered by mutations that reproduce the effects of complexation with the alpha-subunit. The engineered PfTrpB is a powerful platform for production of Trp analogs and for further directed evolution to expand substrate and reaction scope. Directed evolution of the tryptophan synthase beta-subunit for stand-alone function recapitulates allosteric activation.,Buller AR, Brinkmann-Chen S, Romney DK, Herger M, Murciano-Calles J, Arnold FH Proc Natl Acad Sci U S A. 2015 Nov 24;112(47):14599-604. doi:, 10.1073/pnas.1516401112. Epub 2015 Nov 9. PMID:26553994 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tryptophan synthase

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