{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,21]],"date-time":"2026-02-21T00:36:36Z","timestamp":1771634196837,"version":"3.50.1"},"reference-count":45,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2017,6,6]],"date-time":"2017-06-06T00:00:00Z","timestamp":1496707200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2017,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Extracellular nucleoside triphosphate diphosphohydrolases (NTPDases) are enzymes that hydrolyze extracellular nucleotides to the respective monophosphate nucleotides. In the past 20\u00a0years, 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 <jats:italic>Trifolium repens<\/jats:italic> (7WC) and <jats:italic>Vigna unguiculata subsp. cylindrica<\/jats:italic> (DbLNP). Four crystal structures of 7WC and DbLNP were determined at resolutions between 1.9 and 2.6\u00a0\u00c5. For 7WC, structures were determined for an \u2010apo form (1.89\u00a0\u00c5) and with the product AMP (2.15\u00a0\u00c5) and adenine and phosphate (1.76\u00a0\u00c5) bound. For DbLNP, a structure was solved with phosphate and manganese bound (2.60\u00a0\u00c5). 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\u2010factor bound in the active site. A central hinge region creates a \u201cbutterfly\u2010like\u201d motion of the domains that reduces the width of the inter\u2010domain active site cleft upon molecule binding. This phenomenon has been previously described in <jats:italic>Rattus norvegicus<\/jats:italic> and <jats:italic>Legionella pneumophila<\/jats:italic> NTPDaseI and <jats:italic>Toxoplasma gondii<\/jats:italic> NTPDaseIII suggesting a common catalytic mechanism across the domains of life.<\/jats:p>","DOI":"10.1002\/pro.3199","type":"journal-article","created":{"date-parts":[[2017,5,25]],"date-time":"2017-05-25T16:50:54Z","timestamp":1495731054000},"page":"1627-1638","source":"Crossref","is-referenced-by-count":16,"title":["Structures and kinetics for plant nucleoside triphosphate diphosphohydrolases support a domain motion catalytic mechanism"],"prefix":"10.1002","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0999-553X","authenticated-orcid":false,"given":"Emma L.","family":"Summers","sequence":"first","affiliation":[{"name":"School of Science, University of Waikato Private Bag 3105 Hamilton 3240 New Zealand"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mathew H.","family":"Cumming","sequence":"additional","affiliation":[{"name":"Seafood Research Unit, Plant and Food Research PO Box 5114 Port Nelson 7043 New Zealand"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tifany","family":"Oulavallickal","sequence":"additional","affiliation":[{"name":"Biochemistry Department University of Otago PO Box 56 Dunedin 9054 New Zealand"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nicholas J.","family":"Roberts","sequence":"additional","affiliation":[{"name":"AgResearch Grasslands Research Centre Private Bag 11008 Palmerston North New Zealand"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vickery L.","family":"Arcus","sequence":"additional","affiliation":[{"name":"School of Science, University of Waikato Private Bag 3105 Hamilton 3240 New 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