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1k72

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(New page: 200px<br /><applet load="1k72" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k72, resolution 1.80&Aring;" /> '''The X-ray Crystal St...)
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[[Image:1k72.gif|left|200px]]<br /><applet load="1k72" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1k72, resolution 1.80&Aring;" />
 
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'''The X-ray Crystal Structure Of Cel9G Complexed With cellotriose'''<br />
 
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==Overview==
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==The X-ray Crystal Structure Of Cel9G Complexed With cellotriose==
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Complete cellulose degradation is the first step in the use of biomass as, a source of renewable energy. To this end, the engineering of novel, cellulase activity, the activity responsible for the hydrolysis of the, beta-1,4-glycosidic bonds in cellulose, is a topic of great interest. The, high-resolution X-ray crystal structure of a multidomain endoglucanase, from Clostridium cellulolyticum has been determined at a 1.6-A resolution., The endoglucanase, Cel9G, is comprised of a family 9 catalytic domain, attached to a family III(c) cellulose-binding domain. The two domains, together form a flat platform onto which crystalline cellulose is, suggested to bind and be fed into the active-site cleft for endolytic, hydrolysis. To further dissect the structural basis of cellulose binding, and hydrolysis, the structures of Cel9G in the presence of cellobiose, cellotriose, and a DP-10 thio-oligosaccharide inhibitor were resolved at, resolutions of 1.7, 1.8, and 1.9 A, respectively.
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<StructureSection load='1k72' size='340' side='right'caption='[[1k72]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1k72]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ruminiclostridium_cellulolyticum Ruminiclostridium cellulolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K72 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]] 1.8&#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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</scene>, <scene name='pdbligand=SCH:S-METHYL-THIO-CYSTEINE'>SCH</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=1k72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k72 OCA], [https://pdbe.org/1k72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k72 RCSB], [https://www.ebi.ac.uk/pdbsum/1k72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k72 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GUNG_RUMCH GUNG_RUMCH] 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 disaccharide 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/k7/1k72_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=1k72 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Complete cellulose degradation is the first step in the use of biomass as a source of renewable energy. To this end, the engineering of novel cellulase activity, the activity responsible for the hydrolysis of the beta-1,4-glycosidic bonds in cellulose, is a topic of great interest. The high-resolution X-ray crystal structure of a multidomain endoglucanase from Clostridium cellulolyticum has been determined at a 1.6-A resolution. The endoglucanase, Cel9G, is comprised of a family 9 catalytic domain attached to a family III(c) cellulose-binding domain. The two domains together form a flat platform onto which crystalline cellulose is suggested to bind and be fed into the active-site cleft for endolytic hydrolysis. To further dissect the structural basis of cellulose binding and hydrolysis, the structures of Cel9G in the presence of cellobiose, cellotriose, and a DP-10 thio-oligosaccharide inhibitor were resolved at resolutions of 1.7, 1.8, and 1.9 A, respectively.
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==About this Structure==
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X-Ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides.,Mandelman D, Belaich A, Belaich JP, Aghajari N, Driguez H, Haser R J Bacteriol. 2003 Jul;185(14):4127-35. PMID:12837787<ref>PMID:12837787</ref>
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1K72 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_cellulolyticum Clostridium cellulolyticum] with GLC, CBI, CA, MG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K72 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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X-Ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides., Mandelman D, Belaich A, Belaich JP, Aghajari N, Driguez H, Haser R, J Bacteriol. 2003 Jul;185(14):4127-35. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12837787 12837787]
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</div>
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[[Category: Cellulase]]
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<div class="pdbe-citations 1k72" style="background-color:#fffaf0;"></div>
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[[Category: Clostridium cellulolyticum]]
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[[Category: Single protein]]
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[[Category: Aghajari, N.]]
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[[Category: Belaich, A.]]
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[[Category: Belaich, J.P.]]
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[[Category: Driguez, H.]]
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[[Category: Haser, R.]]
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[[Category: Mandelman, D.]]
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[[Category: CA]]
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[[Category: CBI]]
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[[Category: GLC]]
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[[Category: GOL]]
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[[Category: MG]]
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[[Category: (alpha-alpha)6-barrel]]
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[[Category: cellotriose]]
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[[Category: cellulose binding domain]]
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[[Category: endoglucanase]]
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[[Category: family 9]]
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[[Category: x-ray diffraction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:54:07 2007''
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==See Also==
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Ruminiclostridium cellulolyticum]]
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[[Category: Aghajari N]]
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[[Category: Belaich A]]
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[[Category: Belaich JP]]
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[[Category: Driguez H]]
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[[Category: Haser R]]
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[[Category: Mandelman D]]

Current revision

The X-ray Crystal Structure Of Cel9G Complexed With cellotriose

PDB ID 1k72

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