dc.date.accessioned | 2016-01-08T12:04:12Z | |
dc.date.available | 2016-01-08T12:04:12Z | |
dc.date.created | 2015-09-25T14:41:49Z | |
dc.date.issued | 2015 | |
dc.identifier.citation | Naas, Adrian Ertsås Mackenzie, Alasdair Dalhus, Bjørn Eijsink, Vincent Pope, Phillip . Structural features of a Bacteroidetes-affiliated cellulase linked with a polysaccharide utilization locus. Scientific Reports. 2015, 5 | |
dc.identifier.uri | http://hdl.handle.net/10852/48500 | |
dc.description.abstract | 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. | en_US |
dc.language | EN | |
dc.language.iso | en | en_US |
dc.rights | Attribution 4.0 International | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
dc.title | Structural features of a Bacteroidetes-affiliated cellulase linked with a polysaccharide utilization locus | en_US |
dc.type | Journal article | en_US |
dc.creator.author | Naas, Adrian Ertsås | |
dc.creator.author | Mackenzie, Alasdair | |
dc.creator.author | Dalhus, Bjørn | |
dc.creator.author | Eijsink, Vincent | |
dc.creator.author | Pope, Phillip | |
cristin.unitcode | 185,53,18,14 | |
cristin.unitname | Avdeling for medisinsk biokjemi | |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.qualitycode | 1 | |
dc.identifier.cristin | 1275393 | |
dc.identifier.bibliographiccitation | info:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Scientific Reports&rft.volume=5&rft.spage=&rft.date=2015 | |
dc.identifier.jtitle | Scientific Reports | |
dc.identifier.volume | 5 | |
dc.identifier.pagecount | 12 | |
dc.identifier.doi | http://dx.doi.org/10.1038/srep11666 | |
dc.identifier.urn | URN:NBN:no-52407 | |
dc.type.document | Tidsskriftartikkel | en_US |
dc.type.peerreviewed | Peer reviewed | |
dc.source.issn | 2045-2322 | |
dc.identifier.fulltext | Fulltext https://www.duo.uio.no/bitstream/handle/10852/48500/1/ScientificReports11666.pdf | |
dc.type.version | PublishedVersion | |
cristin.articleid | 11666 | |