5a65

Crystal structure of mouse thiamine triphosphatase in complex with thiamine diphosphate, orthophosphate and magnesium ions.

spinqualitylabelsall models 5a65, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a65 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.98Å Ligands: EDO, MG, PO4, TPP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function THTPA_MOUSE Hydrolase highly specific for thiamine triphosphate (ThTP) (By similarity). Publication Abstract from PubMed Triphosphate tunnel metalloenzymes (TTMs) are present in all kingdoms of life and catalyze diverse enzymatic reactions such as mRNA capping, the cyclization of adenosine triphosphate, the hydrolysis of thiamine triphosphate and the synthesis and breakdown of inorganic polyphosphates. TTMs have an unusual tunnel domain fold that harbors substrate- and metal co-factor binding sites. It is presently poorly understood how TTMs specifically sense different triphosphate-containing substrates and how catalysis occurs in the tunnel center. Here we describe substrate-bound structures of inorganic polyphosphatases from Arabidopsis and E. coli, which reveal an unorthodox yet conserved mode of triphosphate and metal co-factor binding. We identify two metal binding sites in these enzymes, with one co-factor involved in substrate coordination and the other in catalysis. Structural comparisons with a substrate- and product-bound mammalian thiamine triphosphatase, and with previously reported structures of mRNA capping enzymes, adenylate cyclases and polyphosphate polymerases, suggest that directionality of substrate binding defines TTM catalytic activity. Our work provides insight into the evolution and functional diversification of an ancient enzyme family. Structural Determinants for Substrate Binding and Catalysis in Triphosphate Tunnel Metalloenzymes.,Martinez J, Truffault V, Hothorn M J Biol Chem. 2015 Jul 28. pii: jbc.M115.674473. PMID:26221030 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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