1rq5

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[[Image:1rq5.jpg|left|200px]]
 
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==Structural Basis for the Exocellulase Activity of the Cellobiohydrolase CbhA from C. thermocellum==
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The line below this paragraph, containing "STRUCTURE_1rq5", creates the "Structure Box" on the page.
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<StructureSection load='1rq5' size='340' side='right'caption='[[1rq5]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_1rq5| PDB=1rq5 | SCENE= }}
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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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'''Structural Basis for the Exocellulase Activity of the Cellobiohydrolase CbhA from C. thermocellum'''
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==See Also==
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*[[Cellobiohydrolase 3D structures|Cellobiohydrolase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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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[[Category: Acetivibrio thermocellus]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Chang J]]
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1RQ5 is a [[Single protein]] structure of 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=1RQ5 OCA].
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[[Category: Kataeva IA]]
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[[Category: Ljungdahl LG]]
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==Reference==
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[[Category: Rose JP]]
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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://www.ncbi.nlm.nih.gov/pubmed/14756552 14756552]
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[[Category: Schubot FD]]
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[[Category: Cellulose 1,4-beta-cellobiosidase]]
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[[Category: Shah AK]]
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[[Category: Clostridium thermocellum]]
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[[Category: Wang BC]]
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[[Category: Single protein]]
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[[Category: Chang, J.]]
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[[Category: Kataeva, I A.]]
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[[Category: Ljungdahl, L G.]]
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[[Category: Rose, J P.]]
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[[Category: Schubot, F D.]]
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[[Category: Shah, A K.]]
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[[Category: Wang, B C.]]
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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 Sat May 3 07:46:53 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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