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2yik
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2yik is ON HOLD Authors: Tsai, J.-Y., Kesavulu, M.M., Hsiao, C.-D. Description: Catalytic domain of Clostridium thermocellum CelT) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Catalytic domain of Clostridium thermocellum CelT== | |
| + | <StructureSection load='2yik' size='340' side='right'caption='[[2yik]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2yik]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YIK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YIK FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2yik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yik OCA], [https://pdbe.org/2yik PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yik RCSB], [https://www.ebi.ac.uk/pdbsum/2yik PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yik ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A3DJ82_ACET2 A3DJ82_ACET2] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cellulases hydrolyze cellulose, a major component of plant cell walls, to oligosaccharides and monosaccharides. Several Clostridium species secrete multi-enzyme complexes (cellulosomes) containing cellulases. C. thermocellum CelT, a family 9 cellulase, lacks the accessory module(s) necessary for activity, unlike most other family 9 cellulases. Therefore, characterization of the CelT structure is essential in order to understand its catalytic mechanism. Here, the crystal structure of free CelTDeltadoc, the catalytic domain of CelT, is reported at 2.1 A resolution. Its structure differs in several aspects from those of other family 9 cellulases. CelTDeltadoc contains an additional alpha-helix, alpha-helices of increased length and two additional surface-exposed beta-strands. It also contains three calcium ions instead of one as found in C. cellulolyticum Cel9M. CelTDeltadoc also has two flexible loops at the open end of its active-site cleft. Movement of these loops probably allows the substrate to access the active site. CelT is stable over a wide range of pH and temperature conditions, suggesting that CelT could be used to convert cellulose biomass into biofuel. | ||
| - | + | Structure of the catalytic domain of the Clostridium thermocellum cellulase CelT.,Kesavulu MM, Tsai JY, Lee HL, Liang PH, Hsiao CD Acta Crystallogr D Biol Crystallogr. 2012 Mar;68(Pt 3):310-20. Epub 2012 Feb 14. PMID:22349233<ref>PMID:22349233</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2yik" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Acetivibrio thermocellus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hsiao C-D]] | ||
| + | [[Category: Kesavulu MM]] | ||
| + | [[Category: Tsai J-Y]] | ||
Current revision
Catalytic domain of Clostridium thermocellum CelT
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