4yhe: Difference between revisions
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New page: '''Unreleased structure''' The entry 4yhe is ON HOLD Authors: Naas, A.E., MacKenzie, A.K., Dalhus, B., Eijsink, V.G.H., Pope, P.B. Description: NATIVE BACTEROIDETES-AFFILIATED GH5 CELL... |
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The | ==NATIVE BACTEROIDETES-AFFILIATED GH5 CELLULASE LINKED WITH A POLYSACCHARIDE UTILIZATION LOCUS== | ||
<StructureSection load='4yhe' size='340' side='right'caption='[[4yhe]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4yhe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroidetes_bacterium_AC2a Bacteroidetes bacterium AC2a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YHE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4yhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yhe OCA], [https://pdbe.org/4yhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yhe RCSB], [https://www.ebi.ac.uk/pdbsum/4yhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yhe ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A076MPD7_9BACT A0A076MPD7_9BACT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 A three-dimensional structure of AC2aCel5A, and characterization of its enzymatic activities. The enzyme possesses the archetypical (beta/alpha)8-barrel found throughout the GH5 family, and contains the two strictly conserved catalytic glutamates located at the C-terminal ends of beta-strands 4 and 7. The enzyme is active on insoluble cellulose and acts exclusively on linear beta-(1,4)-linked glucans. Co-crystallization of a catalytically inactive mutant with substrate yielded a 2.4 A 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. | |||
Structural Features of a Bacteroidetes-Affiliated Cellulase Linked with a Polysaccharide Utilization Locus.,Naas AE, MacKenzie AK, Dalhus B, Eijsink VG, Pope PB Sci Rep. 2015 Jul 2;5:11666. doi: 10.1038/srep11666. PMID:26133573<ref>PMID:26133573</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4yhe" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Naas | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Bacteroidetes bacterium AC2a]] | |||
[[Category: Large Structures]] | |||
[[Category: Dalhus B]] | |||
[[Category: Eijsink VGH]] | |||
[[Category: MacKenzie AK]] | |||
[[Category: Naas AE]] | |||
[[Category: Pope PB]] | |||
Latest revision as of 11:31, 9 May 2024
NATIVE BACTEROIDETES-AFFILIATED GH5 CELLULASE LINKED WITH A POLYSACCHARIDE UTILIZATION LOCUS
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