4yhg: Difference between revisions
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''' | ==NATIVE BACTEROIDETES-AFFILIATED GH5 CELLULASE LINKED WITH A POLYSACCHARIDE UTILIZATION LOCUS== | ||
<StructureSection load='4yhg' size='340' side='right' caption='[[4yhg]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4yhg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YHG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YHG FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CT3:BETA-D-GLUCOPYRANOSYL-(1- 4)-BETA-D-GLUCOPYRANOSYL-(1- 4)-BETA-D-GLUCOPYRANOSE'>CT3</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4yhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yhg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4yhg RCSB], [http://www.ebi.ac.uk/pdbsum/4yhg PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: | [[Category: Cellulase]] | ||
[[Category: Dalhus, B]] | [[Category: Dalhus, B]] | ||
[[Category: Eijsink, V G.H]] | |||
[[Category: MacKenzie, A K]] | |||
[[Category: Naas, A E]] | |||
[[Category: Pope, P B]] | |||
[[Category: Beta alpha barrel]] | |||
[[Category: Glycoside hydrolase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Metagenomic]] | |||
