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1g9j

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[[Image:1g9j.jpg|left|200px]]
 
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{{Structure
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==X-TAL STRUCTURE OF THE MUTANT E44Q OF THE CELLULASE CEL48F IN COMPLEX WITH A THIOOLIGOSACCHARIDE==
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|PDB= 1g9j |SIZE=350|CAPTION= <scene name='initialview01'>1g9j</scene>, resolution 1.90&Aring;
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<StructureSection load='1g9j' size='340' side='right'caption='[[1g9j]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
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<table><tr><td colspan='2'>[[1g9j]] is a 1 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=1G9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G9J FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4]
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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]] 1.9&#8491;</td></tr>
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|GENE=
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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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</scene></td></tr>
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}}
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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=1g9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g9j OCA], [https://pdbe.org/1g9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g9j RCSB], [https://www.ebi.ac.uk/pdbsum/1g9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g9j ProSAT]</span></td></tr>
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</table>
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'''X-TAL STRUCTURE OF THE MUTANT E44Q OF THE CELLULASE CEL48F IN COMPLEX WITH A THIOOLIGOSACCHARIDE'''
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== Function ==
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[https://www.uniprot.org/uniprot/GUNF_RUMCH GUNF_RUMCH] Probable endoglucanase involved in the degradation of cellulose or related beta-glucans.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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An efficient breakdown of lignocellulosic biomass is a prerequisite for the production of second-generation biofuels. Cellulases are key enzymes in this process. We crystallized complexes between hemithio-cello-deca and dodecaoses and the inactive mutants E44Q and E55Q of the endo-processive cellulase Cel48F, one of the most abundant cellulases in cellulosomes from Clostridium cellulolyticum, to elucidate its processive mechanism. In both complexes, the cellooligosaccharides occupy similar positions in the tunnel part of the active site but are more or less buried into the cleft, which hosts the active site. In the E44Q complex, it proceeds along the upper part of the cavity, while it occupies in the E55Q complex the same productive binding subsites in the lower part of the cavity that have previously been reported in Cel48F/cellooligosaccharide complexes. In both cases, the sugar moieties are stabilized by stacking interactions with aromatic side chains and H bonds. The upper pathway is gated by Tyr403, which blocks its access in the E55Q complex and offers a new stacking interaction in the E44Q complex. The new structural data give rise to the hypothesis of a two-step mechanism in which processive action and chain disruption occupy different subsites at the end of their trajectory. In the first part of the mechanism, the chain may smoothly slide up to the leaving group site along the upper pathway, while in the second part, the chain is cleaved in the already described productive binding position located in the lower pathway. The solved native structure of Cel48F without any bound sugar in the active site confirms the two side-chain orientations of the proton donor Glu55 as observed in the complex structures.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g9/1g9j_consurf.spt"</scriptWhenChecked>
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1G9J 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=1G9J OCA].
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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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==Reference==
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</jmolCheckbox>
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Structures of mutants of cellulase Cel48F of Clostridium cellulolyticum in complex with long hemithiocellooligosaccharides give rise to a new view of the substrate pathway during processive action., Parsiegla G, Reverbel C, Tardif C, Driguez H, Haser R, J Mol Biol. 2008 Jan 11;375(2):499-510. Epub 2007 Oct 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18035374 18035374]
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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=1g9j ConSurf].
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[[Category: Clostridium cellulolyticum]]
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<div style="clear:both"></div>
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[[Category: Hydrolase]]
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__TOC__
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[[Category: Single protein]]
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</StructureSection>
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[[Category: Belaich, J P.]]
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[[Category: Large Structures]]
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[[Category: Driguez, H.]]
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[[Category: Ruminiclostridium cellulolyticum]]
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[[Category: Haser, R.]]
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[[Category: Belaich JP]]
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[[Category: Parsiegla, G.]]
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[[Category: Driguez H]]
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[[Category: Tardif, C.]]
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[[Category: Haser R]]
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[[Category: CA]]
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[[Category: Parsiegla G]]
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[[Category: CL]]
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[[Category: Tardif C]]
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[[Category: GLC]]
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[[Category: SGC]]
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[[Category: alpha-alpha-6-barrel]]
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[[Category: cellulase]]
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[[Category: thiooligosaccharide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:20:05 2008''
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Current revision

X-TAL STRUCTURE OF THE MUTANT E44Q OF THE CELLULASE CEL48F IN COMPLEX WITH A THIOOLIGOSACCHARIDE

PDB ID 1g9j

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