{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,1,14]],"date-time":"2025-01-14T05:17:26Z","timestamp":1736831846083,"version":"3.33.0"},"reference-count":26,"publisher":"International Union of Crystallography (IUCr)","issue":"8","license":[{"start":{"date-parts":[[2015,7,28]],"date-time":"2015-07-28T00:00:00Z","timestamp":1438041600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2015,7,28]],"date-time":"2015-07-28T00:00:00Z","timestamp":1438041600000},"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 F Struct Biol Commun","Acta Crystallogr F","Acta Crystallogr F Struct Biol Cryst Commun","Acta Cryst F","Acta Cryst F Struct Biol Commun","Acta Cryst Sect F","Acta Cryst Sect F Struct Biol Commun","Acta Crystallogr Sect F","Acta Crystallogr Sect F Struct Biol Commun","Acta Crystallogr Sect F Struct Biol Cryst Commun"],"published-print":{"date-parts":[[2015,8,1]]},"abstract":"<jats:p>Ruminant herbivores meet their carbon and energy requirements from a symbiotic relationship with cellulosome-producing anaerobic bacteria that efficiently degrade plant cell-wall polysaccharides. The assembly of carbohydrate-active enzymes (CAZymes) into cellulosomes enhances protein stability and enzyme synergistic interactions. Cellulosomes comprise diverse CAZymes displaying a modular architecture in which a catalytic domain is connected,<jats:italic>via<\/jats:italic>linker sequences, to one or more noncatalytic carbohydrate-binding modules (CBMs). CBMs direct the appended catalytic modules to their target substrates, thus facilitating catalysis. The genome of the ruminal cellulolytic bacterium<jats:italic>Ruminococcus flavefaciens<\/jats:italic>strain FD-1 contains over 200 modular proteins containing the cellulosomal signature dockerin module. One of these is an endoglucanase Cel5A comprising two family 5 glycoside hydrolase catalytic modules (GH5) flanking an unclassified CBM (termed CBM-Rf2) and a C-terminal dockerin. This novel CBM-Rf2 has been purified and crystallized, and data from cacodylate-derivative crystals were processed to 1.02 and 1.29\u2005\u00c5 resolution. The crystals belonged to the orthorhombic space group<jats:italic>P<\/jats:italic>2<jats:sub>1<\/jats:sub>2<jats:sub>1<\/jats:sub>2<jats:sub>1<\/jats:sub>. The CBM-Rf2 structure was solved by a single-wavelength anomalous dispersion experiment at the As edge.<\/jats:p>","DOI":"10.1107\/s2053230x15009784","type":"journal-article","created":{"date-parts":[[2015,7,27]],"date-time":"2015-07-27T15:02:35Z","timestamp":1438009355000},"page":"958-961","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":0,"title":["Purification and crystallographic studies of a putative carbohydrate-binding module from the<i>Ruminococcus flavefaciens<\/i>FD-1 endoglucanase Cel5A"],"prefix":"10.1107","volume":"71","author":[{"given":"Ana Jos\u00e9","family":"Pires","sequence":"first","affiliation":[]},{"given":"Teresa","family":"Ribeiro","sequence":"additional","affiliation":[]},{"given":"Andrew","family":"Thompson","sequence":"additional","affiliation":[]},{"given":"Immacolata","family":"Venditto","sequence":"additional","affiliation":[]},{"given":"V\u00e2nia O.","family":"Fernandes","sequence":"additional","affiliation":[]},{"given":"Pedro","family":"Bule","sequence":"additional","affiliation":[]},{"given":"Helena","family":"Santos","sequence":"additional","affiliation":[]},{"given":"Victor D.","family":"Alves","sequence":"additional","affiliation":[]},{"given":"Virginia","family":"Pires","sequence":"additional","affiliation":[]},{"given":"Luis M. 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