2vn5 - Revision history

OCA at 15:25, 13 December 2023

OCA — Wed, 13 Dec 2023 15:25:46 GMT

←Older revision		Revision as of 15:25, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='2vn5' size='340' side='right'caption='[[2vn5]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='2vn5' size='340' side='right'caption='[[2vn5]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vn5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_35319 Atcc 35319~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VN5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VN5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vn5]] is a 4 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=2VN5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VN5 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 1.9Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1g1k\|1g1k]], [[1edg\|1edg]], [[1g43\|1g43]], [[1ehx\|1ehx]], [[2vn6\|2vn6]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=2vn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vn5 OCA], [https://pdbe.org/2vn5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vn5 RCSB], [https://www.ebi.ac.uk/pdbsum/2vn5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vn5 ProSAT]</span></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=2vn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vn5 OCA], [https://pdbe.org/2vn5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vn5 RCSB], [https://www.ebi.ac.uk/pdbsum/2vn5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vn5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~GUNA_CLOCE GUNA_CLOCE~~]] 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 dissaccharide 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.	+	[https://www.uniprot.org/uniprot/Q45996_9FIRM Q45996_9FIRM]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 35319]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bayer~~, E A~~]]	+	[[Category: Ruminiclostridium cellulolyticum]]
-	[[Category: Davies~~, G J~~]]	+	[[Category: Bayer EA]]
-	[[Category: Fierobe~~, H P~~]]	+	[[Category: Davies GJ]]
-	[[Category: Fontes~~, C M.G A~~]]	+	[[Category: Fierobe HP]]
-	[[Category: Gilbert~~, H J~~]]	+	[[Category: Fontes CMGA]]
-	[[Category: Martinez-Fleites, C]]	+	[[Category: Gilbert HJ]]
-	[[Category: Money~~, V A~~]]	+	[[Category: Martinez-Fleites C]]
-	[[Category: Pinheiro~~, B A~~]]	+	[[Category: Money VA]]
-	[[Category: Prates~~, J A.M~~]]	+	[[Category: Pinheiro BA]]
-	[[Category: Proctor~~, M R]]~~	+	[[Category: Prates JAM]]
-	~~[[Category: Carbohydrate metabolism]]~~	+	[[Category: Proctor MR]]
-	~~[[Category: Cell adhesion]]~~	+
-	~~[[Category: Cellulose degradation]]~~	+
-	~~[[Category: Cellulosome]]~~	+
-	~~[[Category: Cohesin]]~~	+
-	~~[[Category: Dockerin]]~~	+
-	~~[[Category: Glycosidase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Polysaccharide degradation~~]]	+

OCA at 11:41, 30 March 2022

OCA — Wed, 30 Mar 2022 11:41:08 GMT

←Older revision		Revision as of 11:41, 30 March 2022
Line 3:		Line 3:
	<StructureSection load='2vn5' size='340' side='right'caption='[[2vn5]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='2vn5' size='340' side='right'caption='[[2vn5]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vn5]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_35319 Atcc 35319]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VN5 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2VN5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vn5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35319 Atcc 35319]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VN5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VN5 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1k\|1g1k]], [[1edg\|1edg]], [[1g43\|1g43]], [[1ehx\|1ehx]], [[2vn6\|2vn6]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1g1k\|1g1k]], [[1edg\|1edg]], [[1g43\|1g43]], [[1ehx\|1ehx]], [[2vn6\|2vn6]]</div></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=2vn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vn5 OCA], [~~http~~://pdbe.org/2vn5 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2vn5 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2vn5 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2vn5 ProSAT]</span></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=2vn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vn5 OCA], [https://pdbe.org/2vn5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vn5 RCSB], [https://www.ebi.ac.uk/pdbsum/2vn5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vn5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/GUNA_CLOCE GUNA_CLOCE]] 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 dissaccharide 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.	+	[[https://www.uniprot.org/uniprot/GUNA_CLOCE GUNA_CLOCE]] 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 dissaccharide 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.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:12, 25 June 2020

OCA — Thu, 25 Jun 2020 08:12:10 GMT

←Older revision		Revision as of 08:12, 25 June 2020
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	==The Clostridium cellulolyticum dockerin displays a dual binding mode for its cohesin partner==		==The Clostridium cellulolyticum dockerin displays a dual binding mode for its cohesin partner==
-	<StructureSection load='2vn5' size='340' side='right' caption='[[2vn5]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='2vn5' size='340' side='right'caption='[[2vn5]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vn5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35319 Atcc 35319]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VN5 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2VN5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vn5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35319 Atcc 35319]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VN5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VN5 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1k\|1g1k]], [[1edg\|1edg]], [[1g43\|1g43]], [[1ehx\|1ehx]], [[2vn6\|2vn6]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1k\|1g1k]], [[1edg\|1edg]], [[1g43\|1g43]], [[1ehx\|1ehx]], [[2vn6\|2vn6]]</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=2vn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vn5 OCA], [http://pdbe.org/2vn5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vn5 RCSB], [http://www.ebi.ac.uk/pdbsum/2vn5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vn5 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=2vn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vn5 OCA], [http://pdbe.org/2vn5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vn5 RCSB], [http://www.ebi.ac.uk/pdbsum/2vn5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vn5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Glucanase\|Glucanase]]	+	*[[Glucanase 3D structures\|Glucanase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Atcc 35319]]		[[Category: Atcc 35319]]
		+	[[Category: Large Structures]]
	[[Category: Bayer, E A]]		[[Category: Bayer, E A]]
	[[Category: Davies, G J]]		[[Category: Davies, G J]]

OCA at 20:38, 19 September 2018

OCA — Wed, 19 Sep 2018 20:38:21 GMT

←Older revision		Revision as of 20:38, 19 September 2018
Line 1:		Line 1:

-	==~~THE CLOSTRIDIUM CELLULOLYTICUM DOCKERIN DISPLAYS A DUAL BINDING MODE FOR ITS COHESIN PARTNER~~==	+	==The Clostridium cellulolyticum dockerin displays a dual binding mode for its cohesin partner==
	<StructureSection load='2vn5' size='340' side='right' caption='[[2vn5]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='2vn5' size='340' side='right' caption='[[2vn5]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vn/2vn5_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vn/2vn5_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>

OCA at 04:05, 5 August 2016

OCA — Fri, 05 Aug 2016 04:05:30 GMT

←Older revision		Revision as of 04:05, 5 August 2016
Line 1:		Line 1:
		+
	==THE CLOSTRIDIUM CELLULOLYTICUM DOCKERIN DISPLAYS A DUAL BINDING MODE FOR ITS COHESIN PARTNER==		==THE CLOSTRIDIUM CELLULOLYTICUM DOCKERIN DISPLAYS A DUAL BINDING MODE FOR ITS COHESIN PARTNER==
	<StructureSection load='2vn5' size='340' side='right' caption='[[2vn5]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='2vn5' size='340' side='right' caption='[[2vn5]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vn5]] is a 4 chain structure with 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=2VN5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VN5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vn5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35319 Atcc 35319]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VN5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VN5 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1k\|1g1k]], [[1edg\|1edg]], [[1g43\|1g43]], [[1ehx\|1ehx]], [[2vn6\|2vn6]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1k\|1g1k]], [[1edg\|1edg]], [[1g43\|1g43]], [[1ehx\|1ehx]], [[2vn6\|2vn6]]</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=2vn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vn5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vn5 RCSB], [http://www.ebi.ac.uk/pdbsum/2vn5 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=2vn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vn5 OCA], [http://pdbe.org/2vn5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vn5 RCSB], [http://www.ebi.ac.uk/pdbsum/2vn5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vn5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	<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=2vn5 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 28:
	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 2vn5" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Clostridium cellulolyticum~~]]	+	[[Category: Atcc 35319]]
	[[Category: Bayer, E A]]		[[Category: Bayer, E A]]
	[[Category: Davies, G J]]		[[Category: Davies, G J]]

OCA at 15:41, 25 December 2014

OCA — Thu, 25 Dec 2014 15:41:48 GMT

←Older revision		Revision as of 15:41, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vn5]] is a 4 chain structure with 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=2VN5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VN5 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vn5]] is a 4 chain structure with 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=2VN5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VN5 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1k\|1g1k]], [[1edg\|1edg]], [[1g43\|1g43]], [[1ehx\|1ehx]], [[2vn6\|2vn6]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1k\|1g1k]], [[1edg\|1edg]], [[1g43\|1g43]], [[1ehx\|1ehx]], [[2vn6\|2vn6]]</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=2vn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vn5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vn5 RCSB], [http://www.ebi.ac.uk/pdbsum/2vn5 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=2vn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vn5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vn5 RCSB], [http://www.ebi.ac.uk/pdbsum/2vn5 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GUNA_CLOCE GUNA_CLOCE]] 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 dissaccharide 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.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Clostridium cellulolyticum]]		[[Category: Clostridium cellulolyticum]]
-	[[Category: Bayer, E A.]]	+	[[Category: Bayer, E A]]
-	[[Category: Davies, G J.]]	+	[[Category: Davies, G J]]
-	[[Category: Fierobe, H P.]]	+	[[Category: Fierobe, H P]]
-	[[Category: Fontes, C M.G A.]]	+	[[Category: Fontes, C M.G A]]
-	[[Category: Gilbert, H J.]]	+	[[Category: Gilbert, H J]]
-	[[Category: Martinez-Fleites, C.]]	+	[[Category: Martinez-Fleites, C]]
-	[[Category: Money, V A.]]	+	[[Category: Money, V A]]
-	[[Category: Pinheiro, B A.]]	+	[[Category: Pinheiro, B A]]
-	[[Category: Prates, J A.M.]]	+	[[Category: Prates, J A.M]]
-	[[Category: Proctor, M R.]]	+	[[Category: Proctor, M R]]
	[[Category: Carbohydrate metabolism]]		[[Category: Carbohydrate metabolism]]
	[[Category: Cell adhesion]]		[[Category: Cell adhesion]]

OCA at 07:23, 29 September 2014

OCA — Mon, 29 Sep 2014 07:23:16 GMT

←Older revision		Revision as of 07:23, 29 September 2014
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-	[[~~Image:~~2vn5.~~png~~\|~~left~~\|200px]]	+	==THE CLOSTRIDIUM CELLULOLYTICUM DOCKERIN DISPLAYS A DUAL BINDING MODE FOR ITS COHESIN PARTNER==
		+	<StructureSection load='2vn5' size='340' side='right' caption='[[2vn5]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2vn5]] is a 4 chain structure with 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=2VN5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VN5 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g1k\|1g1k]], [[1edg\|1edg]], [[1g43\|1g43]], [[1ehx\|1ehx]], [[2vn6\|2vn6]]</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=2vn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vn5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vn5 RCSB], [http://www.ebi.ac.uk/pdbsum/2vn5 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/vn/2vn5_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 ==
		+	The plant cell wall degrading apparatus of anaerobic bacteria includes a large multienzyme complex termed the "cellulosome." The complex assembles through the interaction of enzyme-derived dockerin modules with the multiple cohesin modules of the noncatalytic scaffolding protein. Here we report the crystal structure of the Clostridium cellulolyticum cohesin-dockerin complex in two distinct orientations. The data show that the dockerin displays structural symmetry reflected by the presence of two essentially identical cohesin binding surfaces. In one binding mode, visualized through the A16S/L17T dockerin mutant, the C-terminal helix makes extensive interactions with its cohesin partner. In the other binding mode observed through the A47S/F48T dockerin variant, the dockerin is reoriented by 180 degrees and interacts with the cohesin primarily through the N-terminal helix. Apolar interactions dominate cohesin-dockerin recognition that is centered around a hydrophobic pocket on the surface of the cohesin, formed by Leu-87 and Leu-89, which is occupied, in the two binding modes, by the dockerin residues Phe-19 and Leu-50, respectively. Despite the structural similarity between the C. cellulolyticum and Clostridium thermocellum cohesins and dockerins, there is no cross-specificity between the protein partners from the two organisms. The crystal structure of the C. cellulolyticum complex shows that organism-specific recognition between the protomers is dictated by apolar interactions primarily between only two residues, Leu-17 in the dockerin and the cohesin amino acid Ala-129. The biological significance of the plasticity in dockerin-cohesin recognition, observed here in C. cellulolyticum and reported previously in C. thermocellum, is discussed.

-	~~{{STRUCTURE_2vn5\| PDB=2vn5 \| SCENE= }}~~	+	The Clostridium cellulolyticum dockerin displays a dual binding mode for its cohesin partner.,Pinheiro BA, Proctor MR, Martinez-Fleites C, Prates JA, Money VA, Davies GJ, Bayer EA, Fontesm CM, Fierobe HP, Gilbert HJ J Biol Chem. 2008 Jun 27;283(26):18422-30. Epub 2008 Apr 28. PMID:18445585<ref>PMID:18445585</ref>

-	~~===THE CLOSTRIDIUM CELLULOLYTICUM DOCKERIN DISPLAYS A DUAL BINDING MODE FOR ITS COHESIN PARTNER===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_18445585}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2vn5]] is~~ a ~~4 chain structure with 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=2VN5 OCA].~~	+

	==See Also==		==See Also==
	*[[Glucanase\|Glucanase]]		*[[Glucanase\|Glucanase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:018445585<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Clostridium cellulolyticum]]		[[Category: Clostridium cellulolyticum]]
	[[Category: Bayer, E A.]]		[[Category: Bayer, E A.]]

OCA at 18:28, 20 October 2012

OCA — Sat, 20 Oct 2012 18:28:24 GMT

←Older revision		Revision as of 18:28, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2vn5]] is a 4 chain structure ~~of [[Glucanase]]~~ with 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=2VN5 OCA].	+	[[2vn5]] is a 4 chain structure with 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=2VN5 OCA].

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

OCA at 04:11, 27 July 2012

OCA — Fri, 27 Jul 2012 04:11:35 GMT

←Older revision		Revision as of 04:11, 27 July 2012
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	[[Image:2vn5.png\|left\|200px]]		[[Image:2vn5.png\|left\|200px]]

-	<!--
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-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
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	{{STRUCTURE_2vn5\| PDB=2vn5 \| SCENE= }}		{{STRUCTURE_2vn5\| PDB=2vn5 \| SCENE= }}

	===THE CLOSTRIDIUM CELLULOLYTICUM DOCKERIN DISPLAYS A DUAL BINDING MODE FOR ITS COHESIN PARTNER===		===THE CLOSTRIDIUM CELLULOLYTICUM DOCKERIN DISPLAYS A DUAL BINDING MODE FOR ITS COHESIN PARTNER===

-
-	<!--
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-	(as it appears on PubMed at http://www.pubmed.gov), where 18445585 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_18445585}}		{{ABSTRACT_PUBMED_18445585}}

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	==See Also==		==See Also==
-	*[[Glucanase]]	+	*[[Glucanase\|Glucanase]]

	==Reference==		==Reference==

OCA: Protected "2vn5" [edit=sysop:move=sysop]

OCA — Wed, 24 Aug 2011 05:12:09 GMT

Protected "2vn5" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:12, 24 August 2011