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The crystal structure of a thrombin\u2010like enzyme (TLE) from <jats:italic>Bothrops jararacussu<\/jats:italic> venom (Jararacussin\u2010I) was determined at 2.48 \u00c5 resolution. This is the first crystal structure of a TLE and allows structural comparisons with both the <jats:italic>Agkistrodon contortrix contortrix<\/jats:italic> Protein C Activator and the <jats:italic>Trimeresurus stejnegeri<\/jats:italic> plasminogen activator. Despite the highly conserved overall fold, significant differences in the amino acid compositions and three\u2010dimensional conformations of the loops surrounding the active site significantly alter the molecular topography and charge distribution profile of the catalytic interface. In contrast to other SVSPs, the catalytic interface of Jararacussin\u2010I is highly negatively charged, which contributes to its unique macromolecular selectivity.<\/jats:p>","DOI":"10.1002\/pro.2189","type":"journal-article","created":{"date-parts":[[2012,11,8]],"date-time":"2012-11-08T16:32:24Z","timestamp":1352392344000},"page":"128-132","source":"Crossref","is-referenced-by-count":20,"title":["Crystal structure of Jararacussin\u2010I: The highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin\u2010like enzymes"],"prefix":"10.1002","volume":"22","author":[{"given":"A.","family":"Ullah","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"T. A. C. B.","family":"Souza","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"L. 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