{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T13:36:32Z","timestamp":1791293792556,"version":"4.1.0"},"reference-count":43,"publisher":"International Union of Crystallography (IUCr)","issue":"8","license":[{"start":{"date-parts":[[2015,7,31]],"date-time":"2015-07-31T00:00:00Z","timestamp":1438300800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2015,7,31]],"date-time":"2015-07-31T00:00:00Z","timestamp":1438300800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html#TDM"}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr D Biol Crystallogr","Acta Crystallogr D","Acta Crystallogr D Biol Cryst","Acta Cryst D","Acta Cryst D Biol Crystallogr","Acta Cryst D Biol Cryst","Acta Cryst Sect D","Acta Cryst Sect D Biol Cryst","Acta Crystallogr Sect D","Acta Crystallogr Sect D Biol Crystallogr"],"published-print":{"date-parts":[[2015,8,1]]},"abstract":"<jats:p>\u03b2-1,3-Glucanosyltransferase (EC 2.4.1.\u2013) plays an important role in the formation of branched glucans, as well as in cell-wall assembly and rearrangement in fungi and yeasts. The crystal structures of a novel glycoside hydrolase (GH) family 17 \u03b2-1,3-glucanosyltransferase from<jats:italic>Rhizomucor miehei<\/jats:italic>(<jats:italic>Rm<\/jats:italic>Bgt17A) and the complexes of its active-site mutant (E189A) with two substrates were solved at resolutions of 1.30, 2.30 and 2.27\u2005\u00c5, respectively. The overall structure of<jats:italic>Rm<\/jats:italic>Bgt17A had the characteristic (\u03b2\/\u03b1)<jats:sub>8<\/jats:sub>TIM-barrel fold. The structures of<jats:italic>Rm<\/jats:italic>Bgt17A and other GH family 17 members were compared: it was found that a conserved subdomain located in the region near helix \u03b16 and part of the catalytic cleft in other GH family 17 members was absent in<jats:italic>Rm<\/jats:italic>Bgt17A. Instead, four amino-acid residues exposed to the surface of the enzyme (Tyr135, Tyr136, Glu158 and His172) were found in the reducing terminus of subsite +2 of<jats:italic>Rm<\/jats:italic>Bgt17A, hindering access to the catalytic cleft. This distinct region of<jats:italic>Rm<\/jats:italic>Bgt17A makes its catalytic cleft shorter than those of other reported GH family 17 enzymes. The complex structures also illustrated that<jats:italic>Rm<\/jats:italic>Bgt17A can only provide subsites \u22123 to +2. This structural evidence provides a clear explanation of the catalytic mode of<jats:italic>Rm<\/jats:italic>Bgt17A, in which laminaribiose is released from the reducing end of linear \u03b2-1,3-glucan and the remaining glucan is transferred to the end of another \u03b2-1,3-glucan acceptor. The first crystal structure of a GH family 17 \u03b2-1,3-glucanosyltransferase may be useful in studies of the catalytic mechanism of GH family 17 proteins, and provides a basis for further enzymatic engineering or antifungal drug screening.<\/jats:p>","DOI":"10.1107\/s1399004715011037","type":"journal-article","created":{"date-parts":[[2015,7,31]],"date-time":"2015-07-31T13:53:28Z","timestamp":1438350808000},"page":"1714-1724","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":21,"title":["The first crystal structure of a glycoside hydrolase family 17 \u03b2-1,3-glucanosyltransferase displays a unique catalytic cleft"],"prefix":"10.1107","volume":"71","author":[{"given":"Zhen","family":"Qin","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qiaojuan","family":"Yan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jian","family":"Lei","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shaoqing","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhengqiang","family":"Jiang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shiwang","family":"Wu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"329","published-online":{"date-parts":[[2015,7,31]]},"reference":[{"key":"wa5091_bb1","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Cryst. 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