4br5

Rat NTPDase2 in complex with Zn AMPPNP

spinqualitylabelsall models 4br5, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4br5 is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: ANP, GOL, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed In vertebrates, membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) on the cell surface are responsible for signal conversion and termination in purinergic signaling by extracellular nucleotides. Here we present apo and complex structures of the rat NTPDase2 extracellular domain and Legionella pneumophila NTPDase1, including a high-resolution structure with a transition-state analog. Comparison of ATP and ADP binding modes shows how NTPDases engage the same catalytic site for hydrolysis of nucleoside triphosphates and diphosphates. We find that this dual specificity is achieved at the expense of base specificity. Structural and mutational studies indicate that a conserved active-site water is replaced by the phosphate product immediately after phosphoryl transfer. Partial base specificity for purines in LpNTPDase1 is based on a different intersubunit base binding site for pyrimidine bases. A comparison of the bacterial enzyme in six independent crystal forms shows that NTPDases can undergo a domain closure motion of at least 17 degrees . Crystallographic Snapshots along the Reaction Pathway of Nucleoside Triphosphate Diphosphohydrolases.,Zebisch M, Krauss M, Schafer P, Lauble P, Strater N Structure. 2013 Jul 2. pii: S0969-2126(13)00200-1. doi:, 10.1016/j.str.2013.05.016. PMID:23830739 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ectonucleoside triphosphate diphosphohydrolase

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