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==Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellotetraose== | |||
<StructureSection load='3azt' size='340' side='right' caption='[[3azt]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3azt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima_msb8 Thermotoga maritima msb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AZT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AZT FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3amc|3amc]], [[3amd|3amd]], [[3amg|3amg]], [[3azr|3azr]], [[3azs|3azs]], [[3aof|3aof]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM_1751 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 Thermotoga maritima MSB8])</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=3azt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3azt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3azt RCSB], [http://www.ebi.ac.uk/pdbsum/3azt PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The hyperthermophilic endoglucanase Cel5A from Thermotoga maritima can find applications in lignocellulosic biofuel production, because it catalyzes the hydrolysis of glucan- and mannan-based polysaccharides. Here, we report the crystal structures in apo-form and in complex with three ligands, cellotetraose, cellobiose and mannotriose, at 1.29A to 2.40A resolution. The open carbohydrate-binding cavity which can accommodate oligosaccharide substrates with extensively branched chains explained the dual specificity of the enzyme. Combining our structural information and the previous kinetic data, it is suggested that this enzyme prefers beta-glucosyl and beta-mannosyl moieties at the reducing end and uses two conserved catalytic residues, E253 (nucleophile) and E136 (general acid/base), to hydrolyze the glycosidic bonds. Moreover, our results also suggest that the wide spectrum of Tm_Cel5A substrates might be due to the lack of steric hindrance around the C2-hydroxyl group of the glucose or mannose unit from active-site residues. | |||
Diverse substrate recognition mechanism revealed by Thermotoga maritima Cel5A structures in complex with cellotetraose, cellobiose and mannotriose.,Wu TH, Huang CH, Ko TP, Lai HL, Ma Y, Chen CC, Cheng YS, Liu JR, Guo RT Biochim Biophys Acta. 2011 Dec;1814(12):1832-40. doi:, 10.1016/j.bbapap.2011.07.020. Epub 2011 Aug 4. PMID:21839861<ref>PMID:21839861</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
==See Also== | |||
*[[Glucanase|Glucanase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cellulase]] | [[Category: Cellulase]] | ||
[[Category: Thermotoga maritima msb8]] | [[Category: Thermotoga maritima msb8]] | ||
[[Category: Chen, C C | [[Category: Chen, C C]] | ||
[[Category: Cheng, Y S | [[Category: Cheng, Y S]] | ||
[[Category: Guo, R T | [[Category: Guo, R T]] | ||
[[Category: Huang, C H | [[Category: Huang, C H]] | ||
[[Category: Ko, T P | [[Category: Ko, T P]] | ||
[[Category: Lai, H L | [[Category: Lai, H L]] | ||
[[Category: Liu, J R | [[Category: Liu, J R]] | ||
[[Category: Ma, Y | [[Category: Ma, Y]] | ||
[[Category: Wu, T H | [[Category: Wu, T H]] | ||
[[Category: Biofuel]] | [[Category: Biofuel]] | ||
[[Category: Cellulose]] | [[Category: Cellulose]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Tim barrel]] | [[Category: Tim barrel]] | ||
Revision as of 16:25, 18 December 2014
Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with CellotetraoseDiverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellotetraose
Structural highlights
Publication Abstract from PubMedThe hyperthermophilic endoglucanase Cel5A from Thermotoga maritima can find applications in lignocellulosic biofuel production, because it catalyzes the hydrolysis of glucan- and mannan-based polysaccharides. Here, we report the crystal structures in apo-form and in complex with three ligands, cellotetraose, cellobiose and mannotriose, at 1.29A to 2.40A resolution. The open carbohydrate-binding cavity which can accommodate oligosaccharide substrates with extensively branched chains explained the dual specificity of the enzyme. Combining our structural information and the previous kinetic data, it is suggested that this enzyme prefers beta-glucosyl and beta-mannosyl moieties at the reducing end and uses two conserved catalytic residues, E253 (nucleophile) and E136 (general acid/base), to hydrolyze the glycosidic bonds. Moreover, our results also suggest that the wide spectrum of Tm_Cel5A substrates might be due to the lack of steric hindrance around the C2-hydroxyl group of the glucose or mannose unit from active-site residues. Diverse substrate recognition mechanism revealed by Thermotoga maritima Cel5A structures in complex with cellotetraose, cellobiose and mannotriose.,Wu TH, Huang CH, Ko TP, Lai HL, Ma Y, Chen CC, Cheng YS, Liu JR, Guo RT Biochim Biophys Acta. 2011 Dec;1814(12):1832-40. doi:, 10.1016/j.bbapap.2011.07.020. Epub 2011 Aug 4. PMID:21839861[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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