5u7p

Crystal structure of a nucleoside triphosphate diphosphohydrolase (NTPDase) from the legume Trifolium repens

spinqualitylabelsall models 5u7p, resolution 1.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5u7p is a 1 chain structure with sequence from Trifolium repens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.89Å Ligands: PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B9U139_TRIRP Publication Abstract from PubMed Extracellular nucleoside triphosphate diphosphohydrolases (NTPDases) are enzymes that hydrolyze extracellular nucleotides to the respective monophosphate nucleotides. In the past 20 years, NTPDases belonging to mammalian, parasitic and prokaryotic domains of life have been discovered, cloned and characterized. We reveal the first structures of NTPDases from the legume plant species Trifolium repens (7WC) and Vigna unguiculata subsp. cylindrica (DbLNP). Four crystal structures of 7WC and DbLNP were determined at resolutions between 1.9 and 2.6 A. For 7WC, structures were determined for an -apo form (1.89 A) and with the product AMP (2.15 A) and adenine and phosphate (1.76 A) bound. For DbLNP, a structure was solved with phosphate and manganese bound (2.60 A). Thorough kinetic data and analysis is presented. The structure of 7WC and DbLNP reveals that these NTPDases can adopt two conformations depending on the molecule and co-factor bound in the active site. A central hinge region creates a "butterfly-like" motion of the domains that reduces the width of the inter-domain active site cleft upon molecule binding. This phenomenon has been previously described in Rattus norvegicus and Legionella pneumophila NTPDaseI and Toxoplasma gondii NTPDaseIII suggesting a common catalytic mechanism across the domains of life. Structures and kinetics for plant nucleoside triphosphate diphosphohydrolases support a domain motion catalytic mechanism.,Summers EL, Cumming MH, Oulavallickal T, Roberts NJ, Arcus VL Protein Sci. 2017 Aug;26(8):1627-1638. doi: 10.1002/pro.3199. Epub 2017 Jun 6. PMID:28543850 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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