{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T03:29:21Z","timestamp":1767929361565,"version":"3.49.0"},"reference-count":20,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2015,11,6]],"date-time":"2015-11-06T00:00:00Z","timestamp":1446768000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"name":"Kempe Foundation, Swedstruct"},{"name":"Wallenberg Foundation Swedish Research Council","award":["K2013-67X-13001-15-3"],"award-info":[{"award-number":["K2013-67X-13001-15-3"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2015,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The metalloprotease PrtV from <jats:italic>Vibrio cholerae<\/jats:italic> serves an important function for the ability of bacteria to invade the mammalian host cell. The protein belongs to the family of M6 proteases, with a characteristic zinc ion in the catalytic active site. PrtV constitutes a 918 amino acids (102 kDa) multidomain pre\u2010pro\u2010protein that undergoes several N\u2010 and C\u2010terminal modifications to form a catalytically active protease. We report here the NMR structure of the PrtV N\u2010terminal domain (residues 23\u2013103) that contains two short \u03b1\u2010helices in a coiled coil motif. The helices are held together by a cluster of hydrophobic residues. Approximately 30 residues at the C\u2010terminal end, which were predicted to form a third helical structure, are disordered. These residues are highly conserved within the genus <jats:italic>Vibrio<\/jats:italic>, which suggests that they might be functionally important.<\/jats:p>","DOI":"10.1002\/pro.2815","type":"journal-article","created":{"date-parts":[[2015,10,5]],"date-time":"2015-10-05T09:16:43Z","timestamp":1444036603000},"page":"2076-2080","source":"Crossref","is-referenced-by-count":5,"title":["Structure of the <scp>N<\/scp>\u2010terminal domain of the metalloprotease <scp>P<\/scp>rt<scp>V<\/scp> from <scp><i>V<\/i><\/scp><i>ibrio cholerae<\/i>"],"prefix":"10.1002","volume":"24","author":[{"given":"Aaron","family":"Edwin","sequence":"first","affiliation":[{"name":"Department of Chemistry Ume\u00e5 University Ume\u00e5 SE\u2010901 87 Sweden"},{"name":"Ume\u00e5 Centre for Microbial Research (UCMR), Ume\u00e5 University Ume\u00e5 SE\u2010901 87 Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cecilia","family":"Persson","sequence":"additional","affiliation":[{"name":"Swedish NMR Centre at the University of Gothenburg Gothenburg SE\u201040530 Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maxim","family":"Mayzel","sequence":"additional","affiliation":[{"name":"Swedish NMR Centre at the University of Gothenburg Gothenburg SE\u201040530 Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sun Nyunt","family":"Wai","sequence":"additional","affiliation":[{"name":"Ume\u00e5 Centre for Microbial Research (UCMR), Ume\u00e5 University Ume\u00e5 SE\u2010901 87 Sweden"},{"name":"Department of Molecular Biology Ume\u00e5 University Ume\u00e5 SE\u2010901 87 Sweden"},{"name":"The Laboratory for Molecular Infection Medicine Sweden (MIMS) Ume\u00e5 University Ume\u00e5 SE\u2010901 87 Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anders","family":"\u00d6hman","sequence":"additional","affiliation":[{"name":"Department of Pharmacology and Clinical Neuroscience Ume\u00e5 University Ume\u00e5 SE\u2010901 85 Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"B. 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