1l2a

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[[Image:1l2a.jpg|left|200px]]
 
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==The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the Clostridium thermocellum cellulosome==
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The line below this paragraph, containing "STRUCTURE_1l2a", creates the "Structure Box" on the page.
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<StructureSection load='1l2a' size='340' side='right'caption='[[1l2a]], [[Resolution|resolution]] 2.50&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'>[[1l2a]] is a 6 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=1L2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L2A 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]] 2.5&#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=PRD_900005:beta-cellobiose'>PRD_900005</scene>, <scene name='pdbligand=PRD_900020:beta-cellohexaose'>PRD_900020</scene></td></tr>
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{{STRUCTURE_1l2a| PDB=1l2a | 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=1l2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2a OCA], [https://pdbe.org/1l2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l2a RCSB], [https://www.ebi.ac.uk/pdbsum/1l2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l2a ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GUNS_ACETH GUNS_ACETH] This enzyme catalyzes the exohydrolysis of 1,4-beta-glucosidic linkages in cellulose with a preference for amorphous or crystalline cellulose over carboxymethyl cellulose.<ref>PMID:20967294</ref>
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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/l2/1l2a_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=1l2a ConSurf].
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<div style="clear:both"></div>
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'''The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the Clostridium thermocellum cellulosome'''
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==See Also==
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*[[Cellobiohydrolase 3D structures|Cellobiohydrolase 3D structures]]
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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==Overview==
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== References ==
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Cellobiohydrolase CelS plays an important role in the cellulosome, an active cellulase system produced by the thermophilic anaerobe Clostridium thermocellum. The structures of the catalytic domain of CelS in complex with substrate (cellohexaose) and product (cellobiose) were determined at 2.5 and 2.4 A resolution, respectively. The protein folds into an (alpha/alpha)(6) barrel with a tunnel-shaped substrate-binding region. The conformation of the loops defining the tunnel is intrinsically stable in the absence of substrate, suggesting a model to account for the processive mode of action of family 48 cellobiohydrolases. Structural comparisons with other (alpha/alpha)(6) barrel glycosidases indicate that CelS and endoglucanase CelA, a sequence-unrelated family 8 glycosidase with a groove-shaped substrate-binding region, use the same catalytic machinery to hydrolyze the glycosidic linkage, despite a low sequence similarity and a different endo/exo mode of action. A remarkable feature of the mechanism is the absence, from CelS, of a carboxylic group acting as the base catalyst. The nearly identical arrangement of substrate and functionally important residues in the two active sites strongly suggests an evolutionary relationship between the cellobiohydrolase and endoglucanase families, which can therefore be classified into a new clan of glycoside hydrolases.
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1L2A 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=1L2A OCA].
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[[Category: Acetivibrio thermocellus]]
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[[Category: Large Structures]]
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==Reference==
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[[Category: Alzari PM]]
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The crystal structure and catalytic mechanism of cellobiohydrolase CelS, the major enzymatic component of the Clostridium thermocellum Cellulosome., Guimaraes BG, Souchon H, Lytle BL, David Wu JH, Alzari PM, J Mol Biol. 2002 Jul 12;320(3):587-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12096911 12096911]
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[[Category: Guimaraes BG]]
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[[Category: Cellulase]]
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[[Category: Lytle BL]]
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[[Category: Clostridium thermocellum]]
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[[Category: Souchon H]]
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[[Category: Single protein]]
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[[Category: Wu JHD]]
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[[Category: Alzari, P M.]]
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[[Category: Guimaraes, B G.]]
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[[Category: Lytle, B L.]]
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[[Category: Souchon, H.]]
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[[Category: Wu, J H.D.]]
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[[Category: Alpha/alpha barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:27:30 2008''
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Current revision

The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the Clostridium thermocellum cellulosome

PDB ID 1l2a

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