5b5s: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "5b5s" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
==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> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5b5s" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ishikawa, K]] | |||
[[Category: Watanabe, M]] | [[Category: Watanabe, M]] | ||
[[Category: | [[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
| ||||||||||||
