1kwf
From Proteopedia
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==Atomic Resolution Structure of an Inverting Glycosidase in Complex with Substrate== | ==Atomic Resolution Structure of an Inverting Glycosidase in Complex with Substrate== | ||
| - | <StructureSection load='1kwf' size='340' side='right' caption='[[1kwf]], [[Resolution|resolution]] 0.94Å' scene=''> | + | <StructureSection load='1kwf' size='340' side='right'caption='[[1kwf]], [[Resolution|resolution]] 0.94Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1kwf]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1kwf]] 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=1KWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KWF FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.94Å</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=PRD_900016:beta-cellopentaose'>PRD_900016</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kwf OCA], [https://pdbe.org/1kwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kwf RCSB], [https://www.ebi.ac.uk/pdbsum/1kwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kwf ProSAT]</span></td></tr> |
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/GUNA_ACET2 GUNA_ACET2] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kw/1kwf_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kw/1kwf_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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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=1kwf 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=1kwf ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The crystal structure of Clostridium thermocellum endoglucanase CelA in complex with cellopentaose has been determined at 0.94 A resolution. The oligosaccharide occupies six D-glucosyl-binding subsites, three on either side of the scissile glycosidic linkage. The substrate and product of the reaction occupy different positions at the reducing end of the cleft, where an extended array of hydrogen-bonding interactions with water molecules fosters the departure of the leaving group. Severe torsional strain upon the bound substrate forces a distorted boat(2,5) B conformation for the glucosyl residue bound at subsite -1, which facilitates the formation of an oxocarbenium ion intermediate and might favor the breakage of the sugar ring concomitant with catalysis. | ||
| - | + | ==See Also== | |
| - | + | *[[Glucanase 3D structures|Glucanase 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Acetivibrio thermocellus]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Alzari | + | [[Category: Alzari PM]] |
| - | [[Category: Beguin | + | [[Category: Beguin P]] |
| - | [[Category: Costabel | + | [[Category: Costabel M]] |
| - | [[Category: Guerin | + | [[Category: Guerin DMA]] |
| - | [[Category: Lamzin | + | [[Category: Lamzin V]] |
| - | [[Category: Lascombe | + | [[Category: Lascombe M-B]] |
| - | [[Category: Souchon | + | [[Category: Souchon H]] |
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Current revision
Atomic Resolution Structure of an Inverting Glycosidase in Complex with Substrate
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