{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,18]],"date-time":"2026-01-18T04:46:31Z","timestamp":1768711591842,"version":"3.49.0"},"reference-count":33,"publisher":"International Union of Crystallography (IUCr)","issue":"12","license":[{"start":{"date-parts":[[2016,11,29]],"date-time":"2016-11-29T00:00:00Z","timestamp":1480377600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2016,11,29]],"date-time":"2016-11-29T00:00:00Z","timestamp":1480377600000},"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 Struct Biol","Acta Crystallogr D","Acta Cryst D","Acta Cryst D Struct Biol","Acta Cryst Sect D","Acta Cryst Sect D Struct Biol","Acta Crystallogr Sect D","Acta Crystallogr Sect D Struct Biol","Acta Crystallogr D Biol Crystallogr","Acta Cryst D Biol Cryst"],"published-print":{"date-parts":[[2016,12,1]]},"abstract":"<jats:p>The recent division of the large glycoside hydrolase family 43 (GH43) into subfamilies offers a renewed opportunity to develop structure\u2013function studies aimed at clarifying the molecular determinants of substrate specificity in carbohydrate-degrading enzymes. \u03b1-L-Arabinofuranosidases (EC 3.2.1.55) remove arabinose side chains from heteropolysaccharides such as xylan and arabinan. However, there is some evidence suggesting that arabinofuranosidases are substrate-specific, being unable to display a debranching activity on different polysaccharides. Here, the structure of<jats:italic>Clostridium thermocellum<\/jats:italic>arabinofuranosidase 43A (<jats:italic>Ct<\/jats:italic>Abf43A), which has been shown to act in the removal of arabinose side chains from arabinoxylan but not from pectic arabinan, is reported.<jats:italic>Ct<\/jats:italic>Abf43A belongs to GH43 subfamily 16, the members of which have a restricted capacity to attack xylans. The crystal structure of<jats:italic>Ct<\/jats:italic>Abf43A comprises a five-bladed \u03b2-propeller fold typical of GH43 enzymes.<jats:italic>Ct<\/jats:italic>Abf43A displays a highly compact architecture compatible with its high thermostability. Analysis of<jats:italic>Ct<\/jats:italic>Abf43A along with the other member of GH43 subfamily 16 with known structure, the<jats:italic>Bacillus subtilis<\/jats:italic>arabinofuranosidase BsAXH-m2,3, suggests that the specificity of subfamily 16 for arabinoxylan is conferred by a long surface substrate-binding cleft that is complementary to the xylan backbone. The lack of a curved-shaped carbohydrate-interacting platform precludes GH43 subfamily 16 enzymes from interacting with the nonlinear arabinan scaffold and therefore from deconstructing this polysaccharide.<\/jats:p>","DOI":"10.1107\/s205979831601737x","type":"journal-article","created":{"date-parts":[[2016,11,29]],"date-time":"2016-11-29T18:15:46Z","timestamp":1480443346000},"page":"1281-1289","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":13,"title":["Molecular determinants of substrate specificity revealed by the structure of<i>Clostridium thermocellum<\/i>arabinofuranosidase 43A from glycosyl hydrolase family 43 subfamily 16"],"prefix":"10.1107","volume":"72","author":[{"given":"Arun","family":"Goyal","sequence":"first","affiliation":[]},{"given":"Shadab","family":"Ahmed","sequence":"additional","affiliation":[]},{"given":"Kedar","family":"Sharma","sequence":"additional","affiliation":[]},{"given":"Vikas","family":"Gupta","sequence":"additional","affiliation":[]},{"given":"Pedro","family":"Bule","sequence":"additional","affiliation":[]},{"given":"Victor D.","family":"Alves","sequence":"additional","affiliation":[]},{"given":"Carlos M. 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