1cb2

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(New page: 200px<br /> <applet load="1cb2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cb2, resolution 2.0&Aring;" /> '''CELLOBIOHYDROLASE II...)
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[[Image:1cb2.gif|left|200px]]<br />
 
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<applet load="1cb2" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cb2, resolution 2.0&Aring;" />
 
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'''CELLOBIOHYDROLASE II, CATALYTIC DOMAIN, MUTANT Y169F'''<br />
 
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==Overview==
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==CELLOBIOHYDROLASE II, CATALYTIC DOMAIN, MUTANT Y169F==
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Trichoderma reesei cellobiohydrolase II (CBHII) is an exoglucanase, cleaving primarily cellobiose units from the non-reducing end of cellulose, chains. The beta-1,4 glycosidic bond is cleaved by acid catalysis with an, aspartic acid, D221, as the likely proton donor, and another aspartate, D175, probably ensuring its protonation and stabilizing charged reaction, intermediates. The catalytic base has not yet been identified, experimentally. The refined crystal structure of CBHII also shows a, tyrosine residue, Y169, located close enough to the scissile bond to be, involved in catalysis. The role of this residue has been studied by, introducing a mutation Y169F, and analysing the kinetic and binding, behavior of the mutated CBHII. The crystal structure of the mutated enzyme, was determined ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8875646 (full description)]]
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<StructureSection load='1cb2' size='340' side='right'caption='[[1cb2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cb2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CB2 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&#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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1cb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cb2 OCA], [https://pdbe.org/1cb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cb2 RCSB], [https://www.ebi.ac.uk/pdbsum/1cb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cb2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GUX2_HYPJE GUX2_HYPJE] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
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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/cb/1cb2_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=1cb2 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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1CB2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]] with NAG and MAN as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CB2 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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The active site of Trichoderma reesei cellobiohydrolase II: the role of tyrosine 169., Koivula A, Reinikainen T, Ruohonen L, Valkeajarvi A, Claeyssens M, Teleman O, Kleywegt GJ, Szardenings M, Rouvinen J, Jones TA, Teeri TT, Protein Eng. 1996 Aug;9(8):691-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8875646 8875646]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Trichoderma reesei]]
[[Category: Trichoderma reesei]]
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[[Category: Jones, T.A.]]
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[[Category: Jones TA]]
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[[Category: Kleywegt, G.J.]]
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[[Category: Kleywegt GJ]]
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[[Category: Szardenings, M.]]
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[[Category: Szardenings M]]
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[[Category: MAN]]
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[[Category: NAG]]
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[[Category: glycoprotein]]
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[[Category: glycosidase]]
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[[Category: hydrolase (o-glycosyl)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:24:56 2007''
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Current revision

CELLOBIOHYDROLASE II, CATALYTIC DOMAIN, MUTANT Y169F

PDB ID 1cb2

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