1edg

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[[Image:1edg.gif|left|200px]]
 
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{{Structure
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==SINGLE CRYSTAL STRUCTURE DETERMINATION OF THE CATALYTIC DOMAIN OF CELCCA CARRIED OUT AT 15 DEGREE C==
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|PDB= 1edg |SIZE=350|CAPTION= <scene name='initialview01'>1edg</scene>, resolution 1.6&Aring;
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<StructureSection load='1edg' size='340' side='right'caption='[[1edg]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1edg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ruminiclostridium_cellulolyticum_H10 Ruminiclostridium cellulolyticum H10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EDG FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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]] 1.6&#8491;</td></tr>
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|GENE= CELCCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1521 Clostridium cellulolyticum])
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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=1edg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edg OCA], [https://pdbe.org/1edg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1edg RCSB], [https://www.ebi.ac.uk/pdbsum/1edg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1edg ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1edg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edg OCA], [http://www.ebi.ac.uk/pdbsum/1edg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1edg RCSB]</span>
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[https://www.uniprot.org/uniprot/GUNA_RUMCH GUNA_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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}}
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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/ed/1edg_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=1edg ConSurf].
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<div style="clear:both"></div>
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'''SINGLE CRYSTAL STRUCTURE DETERMINATION OF THE CATALYTIC DOMAIN OF CELCCA CARRIED OUT AT 15 DEGREE C'''
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==See Also==
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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BACKGROUND: Cellulases are glycosyl hydrolases--enzymes that hydrolyze glycosidic bonds. They have been widely studied using biochemical and microbiological techniques and have attracted industrial interest because of their potential in biomass conversion and in the paper and textile industries. Glycosyl hydrolases have lately been assigned to specific families on the basis of similarities in their amino acid sequences. The cellulase endoglucanase A produced by Clostridium cellulolyticum (CelCCA) belongs to family 5. RESULTS: We have determined the crystal structure of the catalytic domain of CelCCA at a resolution of 2.4 A and refined it to 1.6 A. The structure was solved by the multiple isomorphous replacement method. The overall structural fold, (alpha/beta)8, belongs to the TIM barrel motif superfamily. The catalytic centre is located at the C-terminal ends of the beta strands; the aromatic residues, forming the substrate-binding site, are arranged along a long cleft on the surface of the globular enzyme. CONCLUSIONS: Strictly conserved residues within family 5 are described with respect to their catalytic function. The proton donor, Glu170, and the nucleophile, Glu307, are localized on beta strands IV and VII, respectively, and are separated by 5.5 A, as expected for enzymes which retain the configuration of the substrate's anomeric carbon. Structure determination of the catalytic domain of CelCCA allows a comparison with related enzymes belonging to glycosyl hydrolase families 2, 10 and 17, which also display an (alpha/beta)8 fold.
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[[Category: Large Structures]]
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[[Category: Ruminiclostridium cellulolyticum H10]]
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==About this Structure==
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[[Category: Czjzek M]]
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1EDG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_cellulolyticum Clostridium cellulolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDG OCA].
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[[Category: Ducros V]]
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[[Category: Haser R]]
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==Reference==
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Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5., Ducros V, Czjzek M, Belaich A, Gaudin C, Fierobe HP, Belaich JP, Davies GJ, Haser R, Structure. 1995 Sep 15;3(9):939-49. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8535787 8535787]
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[[Category: Cellulase]]
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[[Category: Clostridium cellulolyticum]]
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[[Category: Single protein]]
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[[Category: Czjzek, M.]]
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[[Category: Ducros, V.]]
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[[Category: Haser, R.]]
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[[Category: cellulase]]
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[[Category: cellulose degradation]]
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[[Category: family 5 of glycosyl hydrolase]]
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[[Category: family some]]
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[[Category: xylanase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:00:19 2008''
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Current revision

SINGLE CRYSTAL STRUCTURE DETERMINATION OF THE CATALYTIC DOMAIN OF CELCCA CARRIED OUT AT 15 DEGREE C

PDB ID 1edg

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