4bvp

Legionella pneumophila NTPDase1 crystal form II (closed) in complex with heptamolybdate and octamolybdate

spinqualitylabelsall models 4bvp, resolution 1.49Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bvp is a 2 chain structure with sequence from Legionella pneumophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.49Å Ligands: 6LL, CL, EDO, GOL, M27, MES, MG, MOO, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5ZUA2_LEGPH Publication Abstract from PubMed Nucleoside triphosphate diphosphohydrolases (NTPDases) are secreted or membrane-bound ectonucleotidases that hydrolyze the anhydride bonds of nucleoside triphosphates and nucleoside diphosphates. Mammalian cell-surface NTPDase enzymes are inhibited by various polyoxometallates. Here, the structures of NTPDase1 from the bacterium Legionella pneumophila (LpNTPDase1) in complex with the dodecatungstate POM-1, decavanadate and octamolybdate/heptamolybdate are described. The metal clusters are bound at different sites but always in a highly ordered fashion via electrostatic interactions and hydrogen bonds. For octamolybdate, covalent interactions after oxygen ligand exchange by a serine and histidine side chain are also observed. The potential inhibitory mechanism and the use of the metal clusters as phasing tools for new NTPDase structures are discussed. The binding mode of a tartrate ion at the catalytic centre suggests novel strategies for the structure-based design of NTPDase inhibitors, and the observation of the enzyme in an intermediate open state contributes to our understanding of NTPDase enzyme dynamics. Structures of Legionella pneumophila NTPDase1 in complex with polyoxometallates.,Zebisch M, Krauss M, Schafer P, Strater N Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):1147-54. doi:, 10.1107/S1399004714001916. Epub 2014 Mar 21. PMID:24699658 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ectonucleoside triphosphate diphosphohydrolase

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