4xwn
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Complex structure of catalytic domain of Clostridium Cellulovorans Exgs and Cellotetraose== |
| + | <StructureSection load='4xwn' size='340' side='right' caption='[[4xwn]], [[Resolution|resolution]] 2.88Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4xwn]] 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=4kkk 4kkk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XWN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XWN 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=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xwl|4xwl]], [[4xwm|4xwm]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </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=4xwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xwn OCA], [http://pdbe.org/4xwn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xwn RCSB], [http://www.ebi.ac.uk/pdbsum/4xwn PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Exoglucanase/cellobiohydrolase (EC 3.2.1.176) hydrolyzes a beta-1,4-glycosidic bond from the reducing end of cellulose and releases cellobiose as the major product. Three complex crystal structures of the glycosyl hydrolase 48 (GH48) cellobiohydrolase S (ExgS) from Clostridium cellulovorans with cellobiose, cellotetraose and triethylene glycol molecules were solved. The product cellobiose occupies subsites +1 and +2 in the open active-site cleft of the enzyme-cellotetraose complex structure, indicating an enzymatic hydrolysis function. Moreover, three triethylene glycol molecules and one pentaethylene glycol molecule are located at active-site subsites -2 to -6 in the structure of the ExgS-triethylene glycol complex shown here. Modelling of glucose into subsite -1 in the active site of the ExgS-cellobiose structure revealed that Glu50 acts as a proton donor and Asp222 plays a nucleophilic role. | ||
| - | + | Structures of exoglucanase from Clostridium cellulovorans: cellotetraose binding and cleavage.,Tsai LC, Amiraslanov I, Chen HR, Chen YW, Lee HL, Liang PH, Liaw YC Acta Crystallogr F Struct Biol Commun. 2015 Oct 1;71(Pt 10):1264-72. doi:, 10.1107/S2053230X15015915. Epub 2015 Sep 23. PMID:26457517<ref>PMID:26457517</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 4xwn" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Liaw, Y C]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 04:29, 1 December 2015
Complex structure of catalytic domain of Clostridium Cellulovorans Exgs and Cellotetraose
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