3cja | pdb_00003cja

Structure of Rattus norvegicus NTPDase2 in complex with calcium and AMPPNP

spinqualitylabelsall models 3cja, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3cja 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. Ligands: ANP, CA Related: 3cj1, 3cj7, 3cj9 Gene: Entpd2 (Rattus norvegicus) Activity: Apyrase, with EC number 3.6.1.5 Resources: FirstGlance, OCA, RCSB, PDBsum Function [ENTP2_RAT] In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Cell surface-located nucleoside triphosphate diphosphohydrolases (NTPDase1, -2, -3, and -8) are oligomeric integral membrane proteins responsible for signal conversion and inactivation in extracellular nucleotide-mediated "purinergic" signaling. They catalyze the sequential hydrolysis of the signaling molecule ATP via ADP to AMP. Here we present the structure of the extracellular domain of Rattus norvegicus NTPDase2 in an active state at resolutions between 1.7 A and 2.1 A in four different forms: (i) apo form, (ii) ternary complex with the nonhydrolyzable ATP analog AMPPNP and cofactor Ca(2+), (iii) quaternary complex with Ca(2+) and bound products AMP and phosphate, and (iv) binary product complex with AMP only. Analysis of the ATP (analog) binding mode explains the importance of several residues for activity and allows suggestion of a catalytic mechanism. The carboxylate group of E165 serves as a catalytic base and activates a water molecule, which is well positioned for nucleophilic attack on the terminal phosphate. Based on analysis of the two product complex structures in which AMP adopts different conformations, a substrate binding mode for ADP hydrolysis is proposed. This allows for an understanding of how the same hydrolytic site can be engaged in ATP and ADP but not AMP hydrolysis. Structural insight into signal conversion and inactivation by NTPDase2 in purinergic signaling.,Zebisch M, Strater N Proc Natl Acad Sci U S A. 2008 May 13;105(19):6882-7. Epub 2008 May 5. PMID:18458329 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ectonucleoside triphosphate diphosphohydrolase

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