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It was selected in a structural genomics project as representative of CN hydrolases at a time when no structures had been determined for members of this family. Structures for two other members of the family have since been reported and the three proteins have similar topology and dimerization modes, which are distinct from those of other \u03b1\u03b2\u03b2\u03b1 proteins whose structures are known. The dimers form an unusual eight\u2010layer \u03b1\u03b2\u03b2\u03b1:\u03b1\u03b2\u03b2\u03b1 structure. Although the precise enzymatic reactions catalyzed by the yeast protein are not known, considerable information about the active site may be deduced from conserved sequence motifs, comparative biochemical information, and comparison with known structures of hydrolase active sites. As with serine hydrolases, the active\u2010site nucleophile (cysteine in this case) is positioned on a nucleophile elbow. Proteins 2003;52:283\u2013291. \u00a9 2003 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/prot.10417","type":"journal-article","created":{"date-parts":[[2003,6,24]],"date-time":"2003-06-24T10:16:06Z","timestamp":1056449766000},"page":"283-291","source":"Crossref","is-referenced-by-count":46,"title":["Crystal structure of a putative CN hydrolase from yeast"],"prefix":"10.1002","volume":"52","author":[{"given":"Desigan","family":"Kumaran","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Subramaniam","family":"Eswaramoorthy","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sue Ellen","family":"Gerchman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Helen","family":"Kycia","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"F. 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