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| | <StructureSection load='4yhe' size='340' side='right'caption='[[4yhe]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='4yhe' size='340' side='right'caption='[[4yhe]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4yhe]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YHE FirstGlance]. <br> | + | <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='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=4yhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yhe OCA], [http://pdbe.org/4yhe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yhe RCSB], [http://www.ebi.ac.uk/pdbsum/4yhe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yhe ProSAT]</span></td></tr> | + | </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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A076MPD7_9BACT A0A076MPD7_9BACT] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacteroidetes bacterium ac2a]] | + | [[Category: Bacteroidetes bacterium AC2a]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dalhus, B]] | + | [[Category: Dalhus B]] |
| - | [[Category: Eijsink, V G.H]] | + | [[Category: Eijsink VGH]] |
| - | [[Category: MacKenzie, A K]] | + | [[Category: MacKenzie AK]] |
| - | [[Category: Naas, A E]] | + | [[Category: Naas AE]] |
| - | [[Category: Pope, P B]] | + | [[Category: Pope PB]] |
| - | [[Category: Beta alpha barrel]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Metagenomic]]
| + | |
| Structural highlights
Function
A0A076MPD7_9BACT
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Naas AE, MacKenzie AK, Dalhus B, Eijsink VG, Pope PB. Structural Features of a Bacteroidetes-Affiliated Cellulase Linked with a Polysaccharide Utilization Locus. Sci Rep. 2015 Jul 2;5:11666. doi: 10.1038/srep11666. PMID:26133573 doi:http://dx.doi.org/10.1038/srep11666
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