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The structure of B\u2010form crystals has been solved to 2 \u00c5 resolution, the starting model for which was a 3.5 \u00c5 structure obtained from A\u2010form crystals. The \u03b2\u2010lactamase has an \u03b1 + \u03b2 structure with 11 helices and 5 \u03b2\u2010strands seen also in a peinicilin target <jats:sc>DD<\/jats:sc>\u2010peptidase of <jats:italic>Streptomyces<\/jats:italic> R61.<jats:sup>1<\/jats:sup> Atomic parameters of the two molecules in the asymmetric unit were refined by simulated annealing at 2.0 \u00c5 resolution. The R factor is 0.208 for the 27,330 data greater than 3 (F), with water molecules excluded from the model. The catalytic Ser\u201070 is at the N\u2010terminus of a helix and is within hydrogen bonding distance of conversed Lys\u201073. Also interacting with the Lys\u201073 are Asn\u2010132 and the conserved Glu\u2010166, which is on a potentially flexible helix\u2010containing loop. The structure suggests the binding of \u03b2\u2010lactam substrates is facilitated by interactions with Lys\u2010234, Tyhr\u2010235, and Ala\u2010237 in a conserved \u03b2\u2010strand peptide, which is antiparallel to the \u03b2\u2010lactam's acylamido linkage; an exposed cavity near Asn\u2010170 exits for acylamido Substituent. The reactive double bond of clavulanate\u2010type inhibitors may interact with Arg\u2010244 on the fourth \u03b2\u2010strand. A very similar binding site architecture is seen in the DD\u2010peptidase.<\/jats:p>","DOI":"10.1002\/prot.340070205","type":"journal-article","created":{"date-parts":[[2005,5,29]],"date-time":"2005-05-29T01:05:19Z","timestamp":1117328719000},"page":"156-171","source":"Crossref","is-referenced-by-count":128,"title":["\u03b2\u2010Lactamase of <i>Bacillus licheniformis<\/i> 749\/C at 2 \u00c5 resolution"],"prefix":"10.1002","volume":"7","author":[{"given":"Paul C.","family":"Moews","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James R.","family":"Knox","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Otto","family":"Dideberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paulette","family":"Charlier","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean\u2010Marie","family":"Fr\u00e8re","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2004,2,3]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.3082007"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1080\/02648725.1985.10647814"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.3109\/10408418409105906"},{"key":"e_1_2_1_5_2","unstructured":"Fink A. 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