2yik: Difference between revisions
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[[ | ==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 [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YIK OCA]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xe9|2xe9]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yik OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yik RCSB], [http://www.ebi.ac.uk/pdbsum/2yik PDBsum]</span></td></tr> | |||
<table> | |||
<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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
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[[Category: Cellulase]] | [[Category: Cellulase]] | ||
[[Category: Clostridium thermocellum]] | [[Category: Clostridium thermocellum]] | ||