5b5s
From Proteopedia
(Difference between revisions)
m (Protected "5b5s" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a carbohydrate esterase family 3 from Talaromyces cellulolyticus== | |
| + | <StructureSection load='5b5s' size='340' side='right' caption='[[5b5s]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5b5s]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3x0h 3x0h]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B5S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B5S FirstGlance]. <br> | ||
| + | </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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO3:SULFITE+ION'>SO3</scene></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=5b5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b5s OCA], [http://pdbe.org/5b5s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b5s RCSB], [http://www.ebi.ac.uk/pdbsum/5b5s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b5s ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5b5s" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Ishikawa, K]] | [[Category: Ishikawa, K]] | ||
| + | [[Category: Watanabe, M]] | ||
| + | [[Category: Biomass]] | ||
| + | [[Category: Carbohydrate esterase]] | ||
| + | [[Category: Catalytic triad]] | ||
| + | [[Category: Disulfide bond]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Saccharification xylanase]] | ||
Revision as of 19:25, 9 December 2016
Crystal structure of a carbohydrate esterase family 3 from Talaromyces cellulolyticus
| |||||||||||
