|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='2yik' size='340' side='right'caption='[[2yik]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='2yik' size='340' side='right'caption='[[2yik]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2yik]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"ruminiclostridium_thermocellum"_yutin_and_galperin_2013 "ruminiclostridium thermocellum" yutin and galperin 2013]. 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 [http://proteopedia.org/fgij/fg.htm?mol=2YIK FirstGlance]. <br> | + | <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='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> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xe9|2xe9]]</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2yik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yik OCA], [http://pdbe.org/2yik PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yik RCSB], [http://www.ebi.ac.uk/pdbsum/2yik PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yik ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A3DJ82_ACET2 A3DJ82_ACET2] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ruminiclostridium thermocellum yutin and galperin 2013]] | + | [[Category: Acetivibrio thermocellus]] |
| - | [[Category: Cellulase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hsiao, C D]] | + | [[Category: Hsiao C-D]] |
| - | [[Category: Kesavulu, M M]] | + | [[Category: Kesavulu MM]] |
| - | [[Category: Tsai, J Y]] | + | [[Category: Tsai J-Y]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
A3DJ82_ACET2
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kesavulu MM, Tsai JY, Lee HL, Liang PH, Hsiao CD. Structure of the catalytic domain of the Clostridium thermocellum cellulase CelT. Acta Crystallogr D Biol Crystallogr. 2012 Mar;68(Pt 3):310-20. Epub 2012 Feb 14. PMID:22349233 doi:10.1107/S0907444912001990
|
