1l1y - Revision history

OCA at 07:29, 14 February 2024

OCA — Wed, 14 Feb 2024 07:29:33 GMT

←Older revision		Revision as of 07:29, 14 February 2024
Line 3:		Line 3:
	<StructureSection load='1l1y' size='340' side='right'caption='[[1l1y]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1l1y' size='340' side='right'caption='[[1l1y]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1l1y]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"ruminiclostridium_thermocellum"_(viljoen_et_al._1926)_yutin_and_galperin_2013 "ruminiclostridium thermocellum" (viljoen et al. 1926) yutin and galperin 2013~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L1Y OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1L1Y FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1l1y]] 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=1L1Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L1Y FirstGlance]. <br>
-	</td></tr><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></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.4Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[1l2a\|1l2a]]</div>~~</td></tr>	+	<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></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>cels ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~1515~~ "~~Ruminiclostridium thermocellum~~" ~~(Viljoen et al. 1926) Yutin and Galperin 2013])</td~~><~~/tr>~~	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1y OCA], [https://pdbe.org/1l1y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l1y RCSB], [https://www.ebi.ac.uk/pdbsum/1l1y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l1y ProSAT]</span></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><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~~></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=1l1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1y OCA], [~~http~~://pdbe.org/1l1y PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1l1y RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1l1y PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1l1y ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/~~GUNS_CLOTM GUNS_CLOTM]~~] This enzyme catalyzes the ~~endohydrolysis~~ of 1,4-beta-glucosidic linkages in cellulose~~, lichenin and cereal beta-D-glucans~~.	+	[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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 22:		Line 20:
	</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=1l1y ConSurf].		</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=1l1y ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	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.
-
-	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:12096911<ref>PMID:12096911</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1l1y" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 39:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Cellulase~~]]	+	[[Category: Acetivibrio thermocellus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Alzari~~, P M~~]]	+	[[Category: Alzari PM]]
-	[[Category: Guimaraes~~, B G~~]]	+	[[Category: Guimaraes BG]]
-	[[Category: Lytle~~, B L~~]]	+	[[Category: Lytle BL]]
-	[[Category: Souchon, H]]	+	[[Category: Souchon H]]
-	[[Category: Wu~~, J H.D]]~~	+	[[Category: Wu JHD]]
-	~~[[Category: Alpha/alpha barrel]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 07:53, 25 November 2020

OCA — Wed, 25 Nov 2020 07:53:54 GMT

←Older revision		Revision as of 07:53, 25 November 2020
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	==The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the Clostridium thermocellum cellulosome==		==The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the Clostridium thermocellum cellulosome==
-	<StructureSection load='1l1y' size='340' side='right' caption='[[1l1y]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='1l1y' size='340' side='right'caption='[[1l1y]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1l1y]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Atcc_27405 Atcc 27405~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L1Y OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1L1Y FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1l1y]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"ruminiclostridium_thermocellum"_(viljoen_et_al._1926)_yutin_and_galperin_2013 "ruminiclostridium thermocellum" (viljoen et al. 1926) yutin and galperin 2013]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L1Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1L1Y FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene></td></tr>	+	</td></tr><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></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l2a\|1l2a]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1l2a\|1l2a]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cels ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 ~~ATCC 27405~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cels ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 "Ruminiclostridium thermocellum" (Viljoen et al. 1926) Yutin and Galperin 2013])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1l1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1y OCA], [http://pdbe.org/1l1y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l1y RCSB], [http://www.ebi.ac.uk/pdbsum/1l1y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l1y ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1l1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1y OCA], [http://pdbe.org/1l1y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l1y RCSB], [http://www.ebi.ac.uk/pdbsum/1l1y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l1y ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l1/1l1y_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l1/1l1y_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1l1y" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1l1y" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Cellobiohydrolase 3D structures\|Cellobiohydrolase 3D structures]]
		+	*[[Glucanase 3D structures\|Glucanase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 27405]]
	[[Category: Cellulase]]		[[Category: Cellulase]]
		+	[[Category: Large Structures]]
	[[Category: Alzari, P M]]		[[Category: Alzari, P M]]
	[[Category: Guimaraes, B G]]		[[Category: Guimaraes, B G]]

OCA at 10:52, 18 October 2017

OCA — Wed, 18 Oct 2017 10:52:43 GMT

←Older revision		Revision as of 10:52, 18 October 2017
Line 1:		Line 1:
		+
	==The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the Clostridium thermocellum cellulosome==		==The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the Clostridium thermocellum cellulosome==
	<StructureSection load='1l1y' size='340' side='right' caption='[[1l1y]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1l1y' size='340' side='right' caption='[[1l1y]], [[Resolution\|resolution]] 2.40Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cels ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 ATCC 27405])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cels ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 ATCC 27405])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1y OCA], [http://pdbe.org/1l1y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l1y RCSB], [http://www.ebi.ac.uk/pdbsum/1l1y PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1y OCA], [http://pdbe.org/1l1y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l1y RCSB], [http://www.ebi.ac.uk/pdbsum/1l1y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l1y ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</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/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</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=1l1y ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 30:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1l1y" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1l1y" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Cellobiohydrolase\|Cellobiohydrolase]]
-	*[[Glucanase\|Glucanase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 22:39, 11 September 2015

OCA — Fri, 11 Sep 2015 22:39:22 GMT

←Older revision		Revision as of 22:39, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1l1y' size='340' side='right' caption='[[1l1y]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1l1y' size='340' side='right' caption='[[1l1y]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1l1y]] is a 6 chain structure with 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=1L1Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L1Y FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1l1y]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27405 Atcc 27405]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L1Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L1Y FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l2a\|1l2a]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l2a\|1l2a]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cels ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 ~~Clostridium thermocellum~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cels ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 ATCC 27405])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1l1y RCSB], [http://www.ebi.ac.uk/pdbsum/1l1y PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1y OCA], [http://pdbe.org/1l1y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l1y RCSB], [http://www.ebi.ac.uk/pdbsum/1l1y PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 29:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1l1y" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Atcc 27405]]
	[[Category: Cellulase]]		[[Category: Cellulase]]
-	[[Category: Clostridium thermocellum]]
	[[Category: Alzari, P M]]		[[Category: Alzari, P M]]
	[[Category: Guimaraes, B G]]		[[Category: Guimaraes, B G]]

OCA at 20:23, 25 December 2014

OCA — Thu, 25 Dec 2014 20:23:40 GMT

←Older revision		Revision as of 20:23, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1l1y]] is a 6 chain structure with 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=1L1Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L1Y FirstGlance]. <br>		<table><tr><td colspan='2'>[[1l1y]] is a 6 chain structure with 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=1L1Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L1Y FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l2a\|1l2a]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l2a\|1l2a]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cels ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 Clostridium thermocellum])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cels ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 Clostridium thermocellum])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1l1y RCSB], [http://www.ebi.ac.uk/pdbsum/1l1y PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1l1y RCSB], [http://www.ebi.ac.uk/pdbsum/1l1y PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GUNS_CLOTM GUNS_CLOTM]] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 37:		Line 39:
	[[Category: Cellulase]]		[[Category: Cellulase]]
	[[Category: Clostridium thermocellum]]		[[Category: Clostridium thermocellum]]
-	[[Category: Alzari, P M.]]	+	[[Category: Alzari, P M]]
-	[[Category: Guimaraes, B G.]]	+	[[Category: Guimaraes, B G]]
-	[[Category: Lytle, B L.]]	+	[[Category: Lytle, B L]]
-	[[Category: Souchon, H.]]	+	[[Category: Souchon, H]]
-	[[Category: Wu, J H.D.]]	+	[[Category: Wu, J H.D]]
	[[Category: Alpha/alpha barrel]]		[[Category: Alpha/alpha barrel]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 14:42, 28 September 2014

OCA — Sun, 28 Sep 2014 14:42:14 GMT

←Older revision		Revision as of 14:42, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1l1y.~~png~~\|~~left~~\|200px]]	+	==The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major Enzymatic Component of the Clostridium thermocellum cellulosome==
		+	<StructureSection load='1l1y' size='340' side='right' caption='[[1l1y]], [[Resolution\|resolution]] 2.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1l1y]] is a 6 chain structure with 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=1L1Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L1Y FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1l2a\|1l2a]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cels ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 Clostridium thermocellum])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1l1y RCSB], [http://www.ebi.ac.uk/pdbsum/1l1y PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l1/1l1y_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	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.

-	~~{{STRUCTURE_1l1y\| PDB=1l1y \| SCENE= }}~~	+	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:12096911<ref>PMID:12096911</ref>

-	~~===The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS~~, ~~the Major Enzymatic Component~~ of the ~~Clostridium thermocellum cellulosome===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_12096911}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1l1y]] is a 6 chain structure with 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=1L1Y OCA].~~	+

	==See Also==		==See Also==
	*[[Cellobiohydrolase\|Cellobiohydrolase]]		*[[Cellobiohydrolase\|Cellobiohydrolase]]
	*[[Glucanase\|Glucanase]]		*[[Glucanase\|Glucanase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:012096911<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Cellulase]]		[[Category: Cellulase]]
	[[Category: Clostridium thermocellum]]		[[Category: Clostridium thermocellum]]

OCA at 21:04, 20 October 2012

OCA — Sat, 20 Oct 2012 21:04:24 GMT

←Older revision		Revision as of 21:04, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1l1y]] is a 6 chain structure ~~of [[Cellobiohydrolase]] and [[Glucanase]]~~ with 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=1L1Y OCA].	+	[[1l1y]] is a 6 chain structure with 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=1L1Y OCA].

	==See Also==		==See Also==

OCA: Protected "1l1y" [edit=sysop:move=sysop]

OCA — Fri, 27 Jul 2012 12:30:33 GMT

Protected "1l1y" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:30, 27 July 2012

OCA at 12:30, 27 July 2012

OCA — Fri, 27 Jul 2012 12:30:31 GMT

←Older revision		Revision as of 12:30, 27 July 2012
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-	{{Seed}}
	[[Image:1l1y.png\|left\|200px]]		[[Image:1l1y.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1l1y", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
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	{{STRUCTURE_1l1y\| PDB=1l1y \| SCENE= }}		{{STRUCTURE_1l1y\| PDB=1l1y \| SCENE= }}

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

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_12096911}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 12096911 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_12096911}}		{{ABSTRACT_PUBMED_12096911}}

	==About this Structure==		==About this Structure==
-	~~1L1Y~~ is a 6 ~~chains~~ structure with ~~sequences~~ 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=1L1Y OCA].	+	[[1l1y]] is a 6 chain structure of [[Cellobiohydrolase]] and [[Glucanase]] with 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=1L1Y OCA].
		+
		+	==See Also==
		+	*[[Cellobiohydrolase\|Cellobiohydrolase]]
		+	*[[Glucanase\|Glucanase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~12096911~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012096911</ref><references group="xtra"/>
	[[Category: Cellulase]]		[[Category: Cellulase]]
	[[Category: Clostridium thermocellum]]		[[Category: Clostridium thermocellum]]
Line 32:		Line 24:
	[[Category: Wu, J H.D.]]		[[Category: Wu, J H.D.]]
	[[Category: Alpha/alpha barrel]]		[[Category: Alpha/alpha barrel]]
-		+	[[Category: Hydrolase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Mon Mar 22 14:53:42 2010''~~	+

OCA at 12:53, 22 March 2010

OCA — Mon, 22 Mar 2010 12:53:43 GMT

←Older revision		Revision as of 12:53, 22 March 2010
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	1L1Y is a 6 chains structure of sequences 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=1L1Y OCA].	+	1L1Y is a 6 chains structure with sequences 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=1L1Y OCA].

	==Reference==		==Reference==
Line 33:		Line 33:
	[[Category: Alpha/alpha barrel]]		[[Category: Alpha/alpha barrel]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Feb 18 06~~:06:~~46 2009~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 22 14:53:42 2010''