4dod: Difference between revisions
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==The structure of Cbescii CelA GH9 module== | ==The structure of Cbescii CelA GH9 module== | ||
<StructureSection load='4dod' size='340' side='right' caption='[[4dod]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='4dod' size='340' side='right' caption='[[4dod]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">celA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31899 "Anaerocellum thermophilum" Svetlichnyi VA et al. 1990])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">celA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31899 "Anaerocellum thermophilum" Svetlichnyi VA et al. 1990])</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='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=4dod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dod OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dod RCSB], [http://www.ebi.ac.uk/pdbsum/4dod PDBsum]</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=4dod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dod OCA], [http://pdbe.org/4dod PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dod RCSB], [http://www.ebi.ac.uk/pdbsum/4dod PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dod ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4dod" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 12:58, 11 August 2016
The structure of Cbescii CelA GH9 moduleThe structure of Cbescii CelA GH9 module
Structural highlights
Publication Abstract from PubMedMost fungi and bacteria degrade plant cell walls by secreting free, complementary enzymes that hydrolyze cellulose; however, some bacteria use large enzymatic assemblies called cellulosomes, which recruit complementary enzymes to protein scaffolds. The thermophilic bacterium Caldicellulosiruptor bescii uses an intermediate strategy, secreting many free cellulases that contain multiple catalytic domains. One of these, CelA, comprises a glycoside hydrolase family 9 and a family 48 catalytic domain, as well as three type III cellulose-binding modules. In the saccharification of a common cellulose standard, Avicel, CelA outperforms mixtures of commercially relevant exo- and endoglucanases. From transmission electron microscopy studies of cellulose after incubation with CelA, we report morphological features that suggest that CelA not only exploits the common surface ablation mechanism driven by general cellulase processivity, but also excavates extensive cavities into the surface of the substrate. These results suggest that nature's repertoire of cellulose digestion paradigms remain only partially discovered and understood. Revealing nature's cellulase diversity: the digestion mechanism of Caldicellulosiruptor bescii CelA.,Brunecky R, Alahuhta M, Xu Q, Donohoe BS, Crowley MF, Kataeva IA, Yang SJ, Resch MG, Adams MW, Lunin VV, Himmel ME, Bomble YJ Science. 2013 Dec 20;342(6165):1513-6. doi: 10.1126/science.1244273. PMID:24357319[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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