5a60 | pdb_00005a60

Crystal structure of full-length E. coli ygiF in complex with tripolyphosphate and two magnesium ions

spinqualitylabelsall models 5a60, resolution 1.82Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a60 is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.82Å Ligands: 3PO, EDO, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 3PASE_ECOLI Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi), which could be cytotoxic because of its high affinity for calcium ion, thereby interfering with calcium signaling. It also hydrolyzes slowly thiamine triphosphate (ThTP). YgiF is a specific PPPase, but it contributes only marginally to the total PPPase activity in E.coli, where the main enzyme responsible for hydrolysis of PPPi is inorganic pyrophosphatase (PPase). 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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