1rq5

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[[Image:1rq5.jpg|left|200px]]<br /><applet load="1rq5" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rq5, resolution 2.4&Aring;" />
 
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'''Structural Basis for the Exocellulase Activity of the Cellobiohydrolase CbhA from C. thermocellum'''<br />
 
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==Overview==
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==Structural Basis for the Exocellulase Activity of the Cellobiohydrolase CbhA from C. thermocellum==
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Numerous bacterial and fungal organisms have evolved elaborate sets of modular glycoside hydrolases and similar enzymes aimed at the degradation of polymeric carbohydrates. Presently, on the basis of sequence similarity catalytic modules of these enzymes have been classified into 90 families. Representatives of a particular family display similar fold and catalytic mechanisms. However, within families distinctions occur with regard to enzymatic properties and type of activity against carbohydrate chains. Cellobiohydrolase CbhA from Clostridium thermocellum is a large seven-modular enzyme with a catalytic module belonging to family 9. In contrast to other representatives of that family possessing only endo- and, in few cases, endo/exo-cellulase activities, CbhA is exclusively an exocellulase. The crystal structures of the combination of the immunoglobulin-like module and the catalytic module of CbhA (Ig-GH9_CbhA) and that of an inactive mutant Ig-GH9_CbhA(E795Q) in complex with cellotetraose (CTT) are reported here. The detailed analysis of these structures reveals that, while key catalytic residues and overall fold are conserved in this enzyme and those of other family 9 glycoside hydrolases, the active site of GH9_CbhA is blocked off after the -2 subsite. This feature which is created by an extension and altered conformation of a single loop region explains the inability of the active site of CbhA to accommodate a long cellulose chain and to cut it internally. This altered loop region is responsible for the exocellulolytic activity of the enzyme.
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<StructureSection load='1rq5' size='340' side='right'caption='[[1rq5]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1rq5]] 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=1RQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RQ5 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<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=PRD_900011:beta-cellotetraose'>PRD_900011</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rq5 OCA], [https://pdbe.org/1rq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rq5 RCSB], [https://www.ebi.ac.uk/pdbsum/1rq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rq5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q59325_ACETH Q59325_ACETH]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rq/1rq5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1rq5 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1RQ5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=CTT:'>CTT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQ5 OCA].
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*[[Cellobiohydrolase 3D structures|Cellobiohydrolase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structural basis for the exocellulase activity of the cellobiohydrolase CbhA from Clostridium thermocellum., Schubot FD, Kataeva IA, Chang J, Shah AK, Ljungdahl LG, Rose JP, Wang BC, Biochemistry. 2004 Feb 10;43(5):1163-70. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14756552 14756552]
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[[Category: Acetivibrio thermocellus]]
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[[Category: Cellulose 1,4-beta-cellobiosidase]]
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[[Category: Large Structures]]
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[[Category: Clostridium thermocellum]]
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[[Category: Chang J]]
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[[Category: Single protein]]
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[[Category: Kataeva IA]]
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[[Category: Chang, J.]]
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[[Category: Ljungdahl LG]]
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[[Category: Kataeva, I A.]]
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[[Category: Rose JP]]
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[[Category: Ljungdahl, L G.]]
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[[Category: Schubot FD]]
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[[Category: Rose, J P.]]
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[[Category: Shah AK]]
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[[Category: Schubot, F D.]]
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[[Category: Wang BC]]
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[[Category: Shah, A K.]]
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[[Category: Wang, B C.]]
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[[Category: CA]]
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[[Category: CTT]]
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[[Category: cbha]]
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[[Category: cellobiohydrolase]]
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[[Category: exocellulase]]
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[[Category: family 9]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:27 2008''
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Current revision

Structural Basis for the Exocellulase Activity of the Cellobiohydrolase CbhA from C. thermocellum

PDB ID 1rq5

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