4up2

Crystal structure of Escherichia coli tryptophanase purified from alkaline stressed bacterial culture.

spinqualitylabelsall models 4up2, resolution 2.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4up2 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.78Å Ligands: BME, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C3SLI7_ECOLX Publication Abstract from PubMed Tryptophanase is a bacterial enzyme involved in the degradation of tryptophan to indole, pyruvate and ammonia, which are compounds that are essential for bacterial survival. Tryptophanase is often overexpressed in stressed cultures. Large amounts of endogenous tryptophanase were purified from Escherichia coli BL21 strain overexpressing another recombinant protein. Tryptophanase was crystallized in space group P6522 in the apo form without pyridoxal 5'-phosphate bound in the active site. Structure of Escherichia coli tryptophanase purified from an alkaline-stressed bacterial culture.,Rety S, Deschamps P, Leulliot N Acta Crystallogr F Struct Biol Commun. 2015 Nov 1;71(Pt 11):1378-83. doi:, 10.1107/S2053230X15017549. Epub 2015 Oct 23. PMID:26527264 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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