| http://purl.uniprot.org/citations/26133573 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26133573 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26133573 | http://www.w3.org/2000/01/rdf-schema#comment | "Previous gene-centric analysis of a cow rumen metagenome revealed the first potentially cellulolytic polysaccharide utilization locus, of which the main catalytic enzyme (AC2aCel5A) was identified as a glycoside hydrolase (GH) family 5 endo-cellulase. Here we present the 1.8 Å three-dimensional structure of AC2aCel5A, and characterization of its enzymatic activities. The enzyme possesses the archetypical (β/α)8-barrel found throughout the GH5 family, and contains the two strictly conserved catalytic glutamates located at the C-terminal ends of β-strands 4 and 7. The enzyme is active on insoluble cellulose and acts exclusively on linear β-(1,4)-linked glucans. Co-crystallization of a catalytically inactive mutant with substrate yielded a 2.4 Å structure showing cellotriose bound in the -3 to -1 subsites. Additional electron density was observed between Trp178 and Trp254, two residues that form a hydrophobic "clamp", potentially interacting with sugars at the +1 and +2 subsites. The enzyme's active-site cleft was narrower compared to the closest structural relatives, which in contrast to AC2aCel5A, are also active on xylans, mannans and/or xyloglucans. Interestingly, the structure and function of this enzyme seem adapted to less-substituted substrates such as cellulose, presumably due to the insufficient space to accommodate the side-chains of branched glucans in the active-site cleft."xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.org/dc/terms/identifier | "doi:10.1038/srep11666"xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.org/dc/terms/identifier | "doi:10.1038/srep11666"xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/author | "Dalhus B."xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/author | "Dalhus B."xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/author | "Eijsink V.G."xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/author | "Eijsink V.G.H."xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/author | "Pope P.B."xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/author | "Pope P.B."xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/author | "Naas A.E."xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/author | "Naas A.E."xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/author | "MacKenzie A.K."xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/author | "MacKenzie A.K."xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/name | "Sci. Rep."xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/name | "Sci Rep"xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/pages | "11666"xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/pages | "11666"xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/title | "Structural Features of a Bacteroidetes-Affiliated Cellulase Linked with a Polysaccharide Utilization Locus."xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/title | "Structural Features of a Bacteroidetes-Affiliated Cellulase Linked with a Polysaccharide Utilization Locus."xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/volume | "5"xsd:string |
| http://purl.uniprot.org/citations/26133573 | http://purl.uniprot.org/core/volume | "5"xsd:string |