2eo7
From Proteopedia
(Difference between revisions)
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==Crystal structure of Cel44A, GH family 44 endoglucanase from Clostridium thermocellum== | ==Crystal structure of Cel44A, GH family 44 endoglucanase from Clostridium thermocellum== | ||
| - | <StructureSection load='2eo7' size='340' side='right'caption='[[2eo7]]' scene=''> | + | <StructureSection load='2eo7' size='340' side='right'caption='[[2eo7]], [[Resolution|resolution]] 1.75Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EO7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2eo7]] 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=2EO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EO7 FirstGlance]. <br> |
| - | </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=2eo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eo7 OCA], [https://pdbe.org/2eo7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eo7 RCSB], [https://www.ebi.ac.uk/pdbsum/2eo7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eo7 ProSAT]</span></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]] 1.75Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRD_900011:beta-cellotetraose'>PRD_900011</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=2eo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eo7 OCA], [https://pdbe.org/2eo7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eo7 RCSB], [https://www.ebi.ac.uk/pdbsum/2eo7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eo7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/P71140_ACETH P71140_ACETH] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2eo7 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2eo7 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The crystal structure of Cel44A, which is one of the enzymatic components of the cellulosome of Clostridium thermocellum, was solved at a resolution of 0.96 A. This enzyme belongs to glycoside hydrolase family (GH family) 44. The structure reveals that Cel44A consists of a TIM-like barrel domain and a beta-sandwich domain. The wild-type and the E186Q mutant structures complexed with substrates suggest that two glutamic acid residues, Glu(186) and Glu(359), are the active residues of the enzyme. Biochemical experiments were performed to confirm this idea. The structural features indicate that GH family 44 belongs to clan GH-A and that the reaction catalyzed by Cel44A is retaining type hydrolysis. The stereochemical course of hydrolysis was confirmed by a (1)H NMR experiment using the reduced cellooligosaccharide as a substrate. | ||
| + | |||
| + | Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum.,Kitago Y, Karita S, Watanabe N, Kamiya M, Aizawa T, Sakka K, Tanaka I J Biol Chem. 2007 Dec 7;282(49):35703-11. Epub 2007 Sep 28. PMID:17905739<ref>PMID:17905739</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2eo7" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Glucanase 3D structures|Glucanase 3D structures]] | *[[Glucanase 3D structures|Glucanase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Acetivibrio thermocellus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Karita S]] | [[Category: Karita S]] | ||
Current revision
Crystal structure of Cel44A, GH family 44 endoglucanase from Clostridium thermocellum
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