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| - | ==Crystal structure of a carbohydrate esterase family 1 from Talaromyces cellulolyticus==
| + | #REDIRECT [[5b5s]] This PDB entry is obsolete and replaced by 5b5s |
| - | <StructureSection load='3x0h' size='340' side='right' caption='[[3x0h]], [[Resolution|resolution]] 1.50Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[3x0h]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3X0H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3X0H FirstGlance]. <br>
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| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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| - | <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=3x0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x0h OCA], [http://pdbe.org/3x0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3x0h RCSB], [http://www.ebi.ac.uk/pdbsum/3x0h PDBsum]</span></td></tr>
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| - | </table>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Carbohydrate esterase catalyzes the de-O or de-N-acylation of substituted saccharides in plant cell walls and thus has great potential for industrial biomass saccharification. We recently identified the putative carbohydrate esterase family 3 (CE3) from Talaromyces cellulolyticus. Here, we prepared the recombinant catalytic domain of the enzyme and crystallized it. The crystal structure was determined to 1.5 A resolution. From the structural analysis, it was elucidated that a n-octyl-beta-D-glucopyranoside bound to near the catalytic triad (Ser10, Asp179 and His182) and was buried in the active site cavity. Site-directed mutagenesis showed that the N-terminal disulfide bond located near the catalytic triad is involved in the activity and structural stability of the enzyme.
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| - | Crystal structure of an acetylesterase from Talaromyces cellulolyticus and the importance of a disulfide bond near the active site.,Watanabe M, Fukada H, Inoue H, Ishikawa K FEBS Lett. 2015 May 8;589(11):1200-6. doi: 10.1016/j.febslet.2015.03.020. Epub, 2015 Mar 28. PMID:25825334<ref>PMID:25825334</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3x0h" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Ishikawa, K]]
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| - | [[Category: Watanabe, M]]
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| - | [[Category: Hydrolase]]
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