4dod: Difference between revisions
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==The structure of Cbescii CelA GH9 module== | |||
=== | <StructureSection load='4dod' size='340' side='right' caption='[[4dod]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4dod]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"anaerocellum_thermophilum"_svetlichnyi_va_et_al._1990 "anaerocellum thermophilum" svetlichnyi va et al. 1990]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DOD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DOD FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4doe|4doe]]</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='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> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Most 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<ref>PMID:24357319</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Glucanase|Glucanase]] | *[[Glucanase|Glucanase]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Anaerocellum thermophilum svetlichnyi va et al. 1990]] | [[Category: Anaerocellum thermophilum svetlichnyi va et al. 1990]] | ||
[[Category: Cellulase]] | [[Category: Cellulase]] | ||
[[Category: Alahuhta, P M | [[Category: Alahuhta, P M]] | ||
[[Category: Lunin, V V | [[Category: Lunin, V V]] | ||
[[Category: Cela]] | [[Category: Cela]] | ||
[[Category: Gh9]] | [[Category: Gh9]] | ||
[[Category: Glycoside hydrolase]] | [[Category: Glycoside hydrolase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 16:43, 4 January 2015
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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