{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,4]],"date-time":"2025-11-04T22:28:14Z","timestamp":1762295294942,"version":"3.33.0"},"reference-count":33,"publisher":"International Union of Crystallography (IUCr)","issue":"12","license":[{"start":{"date-parts":[[2016,11,25]],"date-time":"2016-11-25T00:00:00Z","timestamp":1480032000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/2.0\/uk\/legalcode"},{"start":{"date-parts":[[2016,11,25]],"date-time":"2016-11-25T00:00:00Z","timestamp":1480032000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/2.0\/uk\/legalcode"}],"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":[[2016,12,1]]},"abstract":"<jats:p>Cellulases are produced by microorganisms that grow on cellulose biomass. Here, a cellulase, Cel10, was identified in a strain of<jats:italic>Klebsiella pneumoniae<\/jats:italic>isolated from Chinese bamboo rat gut. Analysis of substrate specificity showed that Cel10 is able to hydrolyze amorphous carboxymethyl cellulose (CMC) and crystalline forms of cellulose (Avicel and xylan) but is unable to hydrolyze<jats:italic>p<\/jats:italic>-nitrophenol \u03b2-D-glucopyranoside (<jats:italic>p<\/jats:italic>-NPG), proving that Cel10 is an endoglucanase. A phylogenetic tree analysis indicates that Cel10 belongs to the glycoside hydrolase 8 (GH8) subfamily. In order to further understanding of its substrate specificity, the structure of Cel10 was solved by molecular replacement and refined to 1.76\u2005\u00c5 resolution. The overall fold is distinct from those of most other enzymes belonging to the GH8 subfamily. Although it forms the typical (\u03b1\/\u03b1)<jats:sub>6<\/jats:sub>-barrel motif fold, like<jats:italic>Acetobacterxylinum<\/jats:italic>CMCax, one helix is missing. Structural comparisons with<jats:italic>Clostridium thermocellum<\/jats:italic>CelA (CtCelA), the best characterized GH8 endoglucanase, revealed that sugar-recognition subsite \u22123 is completely missing in Cel10. The absence of this subsite correlates to a more open substrate-binding cleft on the cellooligosaccharide reducing-end side.<\/jats:p>","DOI":"10.1107\/s2053230x16017891","type":"journal-article","created":{"date-parts":[[2016,11,25]],"date-time":"2016-11-25T16:23:20Z","timestamp":1480091000000},"page":"870-876","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":11,"title":["The crystal structure of the endoglucanase Cel10, a family 8 glycosyl hydrolase from<i>Klebsiella pneumoniae<\/i>"],"prefix":"10.1107","volume":"72","author":[{"given":"Ayman","family":"Attigani","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lifang","family":"Sun","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Qing","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yadan","family":"Liu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dingping","family":"Bai","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shengping","family":"Li","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiaohong","family":"Huang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"329","published-online":{"date-parts":[[2016,11,25]]},"reference":[{"key":"hv5341_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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