3e76 - Revision history

OCA at 12:59, 30 August 2023

OCA — Wed, 30 Aug 2023 12:59:08 GMT

←Older revision		Revision as of 12:59, 30 August 2023
Line 3:		Line 3:
	<StructureSection load='3e76' size='340' side='right'caption='[[3e76]], [[Resolution\|resolution]] 3.94Å' scene=''>		<StructureSection load='3e76' size='340' side='right'caption='[[3e76]], [[Resolution\|resolution]] 3.94Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3e76]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Ecout Ecout~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E76 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3e76]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_UTI89 Escherichia coli UTI89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E76 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID~~-~~ADENYLATE+ESTER'>AGS</scene>~~, ~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</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]] 3.94Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[2nwc\|2nwc]], [[1xck\|1xck]], [[1kp8\|1kp8]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</scene></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">groL~~, ~~groEL, UTI89_C4741 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=364106 ECOUT])~~<~~/td></tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Chaperonin_ATPase Chaperonin ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.9 3.6.4.9]~~ </~~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=3e76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e76 OCA], [https://pdbe.org/3e76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e76 RCSB], [https://www.ebi.ac.uk/pdbsum/3e76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e76 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=3e76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e76 OCA], [https://pdbe.org/3e76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e76 RCSB], [https://www.ebi.ac.uk/pdbsum/3e76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e76 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CH60_ECOUT CH60_ECOUT]] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).	+	[https://www.uniprot.org/uniprot/CH60_ECOUT CH60_ECOUT] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 31:

	==See Also==		==See Also==
-	*[[Chaperonin 3D structures\|Chaperonin 3D structures]]
	*[[Heat Shock Protein structures\|Heat Shock Protein structures]]		*[[Heat Shock Protein structures\|Heat Shock Protein structures]]
	== References ==		== References ==
Line 39:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Chaperonin ATPase]]~~	+	[[Category: Escherichia coli UTI89]]
-	~~[[Category: Ecout~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Kiser~~, P D~~]]	+	[[Category: Kiser PD]]
-	[[Category: Lorimer~~, G H~~]]	+	[[Category: Lorimer GH]]
-	[[Category: Palczewski, K]]	+	[[Category: Palczewski K]]
-	~~[[Category: Atp-binding]]~~	+
-	~~[[Category: Chaperone]]~~	+
-	~~[[Category: Chaperonin]]~~	+
-	~~[[Category: Groel]]~~	+
-	~~[[Category: Hsp60]]~~	+
-	~~[[Category: Nucleotide-binding]]~~	+
-	~~[[Category: Thallium~~]]	+

OCA at 11:41, 16 February 2022

OCA — Wed, 16 Feb 2022 11:41:59 GMT

←Older revision		Revision as of 11:41, 16 February 2022
Line 1:		Line 1:

	==Crystal structure of Wild-type GroEL with bound Thallium ions==		==Crystal structure of Wild-type GroEL with bound Thallium ions==
-	<StructureSection load='3e76' size='340' side='right' caption='[[3e76]], [[Resolution\|resolution]] 3.94Å' scene=''>	+	<StructureSection load='3e76' size='340' side='right'caption='[[3e76]], [[Resolution\|resolution]] 3.94Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3e76]] is a 14 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Ecout Ecout]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3E76 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3e76]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecout Ecout]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E76 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2nwc\|2nwc]], [[1xck\|1xck]], [[1kp8\|1kp8]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2nwc\|2nwc]], [[1xck\|1xck]], [[1kp8\|1kp8]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">groL, groEL, UTI89_C4741 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=364106 ECOUT])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">groL, groEL, UTI89_C4741 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=364106 ECOUT])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Chaperonin_ATPase Chaperonin ATPase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.9 3.6.4.9] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chaperonin_ATPase Chaperonin ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.9 3.6.4.9] </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=3e76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e76 OCA], [~~http~~://pdbe.org/3e76 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3e76 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3e76 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3e76 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=3e76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e76 OCA], [https://pdbe.org/3e76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e76 RCSB], [https://www.ebi.ac.uk/pdbsum/3e76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e76 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CH60_ECOUT CH60_ECOUT]] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).	+	[[https://www.uniprot.org/uniprot/CH60_ECOUT CH60_ECOUT]] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 33:

	==See Also==		==See Also==
-	*[[Chaperonin\|Chaperonin]]	+	*[[Chaperonin 3D structures\|Chaperonin 3D structures]]
-	*[[Heat Shock ~~Proteins~~\|Heat Shock ~~Proteins~~]]	+	*[[Heat Shock Protein structures\|Heat Shock Protein structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 41:		Line 41:
	[[Category: Chaperonin ATPase]]		[[Category: Chaperonin ATPase]]
	[[Category: Ecout]]		[[Category: Ecout]]
		+	[[Category: Large Structures]]
	[[Category: Kiser, P D]]		[[Category: Kiser, P D]]
	[[Category: Lorimer, G H]]		[[Category: Lorimer, G H]]

OCA at 21:20, 2 December 2018

OCA — Sun, 02 Dec 2018 21:20:36 GMT

←Older revision		Revision as of 21:20, 2 December 2018
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/e7/3e76_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e7/3e76_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 18:14, 5 August 2016

OCA — Fri, 05 Aug 2016 18:14:15 GMT

←Older revision		Revision as of 18:14, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of Wild-type GroEL with bound Thallium ions==		==Crystal structure of Wild-type GroEL with bound Thallium ions==
	<StructureSection load='3e76' size='340' side='right' caption='[[3e76]], [[Resolution\|resolution]] 3.94Å' scene=''>		<StructureSection load='3e76' size='340' side='right' caption='[[3e76]], [[Resolution\|resolution]] 3.94Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3e76]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli_uti89 Escherichia coli uti89~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E76 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3e76]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecout Ecout]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E76 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2nwc\|2nwc]], [[1xck\|1xck]], [[1kp8\|1kp8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2nwc\|2nwc]], [[1xck\|1xck]], [[1kp8\|1kp8]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">groL, groEL, UTI89_C4741 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=364106 ~~Escherichia coli UTI89~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">groL, groEL, UTI89_C4741 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=364106 ECOUT])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chaperonin_ATPase Chaperonin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.9 3.6.4.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chaperonin_ATPase Chaperonin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.9 3.6.4.9] </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=3e76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e76 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e76 RCSB], [http://www.ebi.ac.uk/pdbsum/3e76 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=3e76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e76 OCA], [http://pdbe.org/3e76 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e76 RCSB], [http://www.ebi.ac.uk/pdbsum/3e76 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3e76 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=3e76 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 30:
	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 3e76" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Chaperonin ATPase]]		[[Category: Chaperonin ATPase]]
-	[[Category: ~~Escherichia coli uti89~~]]	+	[[Category: Ecout]]
	[[Category: Kiser, P D]]		[[Category: Kiser, P D]]
	[[Category: Lorimer, G H]]		[[Category: Lorimer, G H]]

OCA at 20:53, 25 December 2014

OCA — Thu, 25 Dec 2014 20:53:32 GMT

←Older revision		Revision as of 20:53, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3e76]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_uti89 Escherichia coli uti89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E76 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3e76]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_uti89 Escherichia coli uti89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E76 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2nwc\|2nwc]], [[1xck\|1xck]], [[1kp8\|1kp8]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2nwc\|2nwc]], [[1xck\|1xck]], [[1kp8\|1kp8]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">groL, groEL, UTI89_C4741 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=364106 Escherichia coli UTI89])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">groL, groEL, UTI89_C4741 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=364106 Escherichia coli UTI89])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chaperonin_ATPase Chaperonin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.9 3.6.4.9] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chaperonin_ATPase Chaperonin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.9 3.6.4.9] </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=3e76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e76 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e76 RCSB], [http://www.ebi.ac.uk/pdbsum/3e76 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=3e76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e76 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e76 RCSB], [http://www.ebi.ac.uk/pdbsum/3e76 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CH60_ECOUT CH60_ECOUT]] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 37:		Line 39:
	[[Category: Chaperonin ATPase]]		[[Category: Chaperonin ATPase]]
	[[Category: Escherichia coli uti89]]		[[Category: Escherichia coli uti89]]
-	[[Category: Kiser, P D.]]	+	[[Category: Kiser, P D]]
-	[[Category: Lorimer, G H.]]	+	[[Category: Lorimer, G H]]
-	[[Category: Palczewski, K.]]	+	[[Category: Palczewski, K]]
	[[Category: Atp-binding]]		[[Category: Atp-binding]]
	[[Category: Chaperone]]		[[Category: Chaperone]]

OCA at 10:49, 29 September 2014

OCA — Mon, 29 Sep 2014 10:49:21 GMT

←Older revision		Revision as of 10:49, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~3e76.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of Wild-type GroEL with bound Thallium ions==
		+	<StructureSection load='3e76' size='340' side='right' caption='[[3e76]], [[Resolution\|resolution]] 3.94Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3e76]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_uti89 Escherichia coli uti89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E76 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2nwc\|2nwc]], [[1xck\|1xck]], [[1kp8\|1kp8]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">groL, groEL, UTI89_C4741 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=364106 Escherichia coli UTI89])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chaperonin_ATPase Chaperonin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.9 3.6.4.9] </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=3e76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e76 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e76 RCSB], [http://www.ebi.ac.uk/pdbsum/3e76 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/e7/3e76_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 ==
		+	GroEL is a bacterial chaperone protein that assembles into a homotetradecameric complex exhibiting D(7) symmetry and utilizes the co-chaperone protein GroES and ATP hydrolysis to assist in the proper folding of a variety of cytosolic proteins. GroEL utilizes two metal cofactors, Mg(2+) and K(+), to bind and hydrolyze ATP. A K(+)-binding site has been proposed to be located next to the nucleotide-binding site, but the available structural data do not firmly support this conclusion. Moreover, more than one functionally significant K(+)-binding site may exist within GroEL. Because K(+) has important and complex effects on GroEL activity and is involved in both positive (intra-ring) and negative (inter-ring) cooperativity for ATP hydrolysis, it is important to determine the exact location of these cation-binding site(s) within GroEL. In this study, the K(+) mimetic Tl(+) was incorporated into GroEL crystals, a moderately redundant 3.94 A resolution X-ray diffraction data set was collected from a single crystal and the strong anomalous scattering signal from the thallium ion was used to identify monovalent cation-binding sites. The results confirmed the previously proposed placement of K(+) next to the nucleotide-binding site and also identified additional binding sites that may be important for GroEL function and cooperativity. These findings also demonstrate the general usefulness of Tl(+) for the identification of monovalent cation-binding sites in protein crystal structures, even when the quality and resolution of the diffraction data are relatively low.

-	~~{{STRUCTURE_3e76\| PDB=3e76 \| SCENE= }}~~	+	Use of thallium to identify monovalent cation binding sites in GroEL.,Kiser PD, Lorimer GH, Palczewski K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Oct 1;65(Pt, 10):967-71. Epub 2009 Sep 18. PMID:19851000<ref>PMID:19851000</ref>

-	~~===Crystal structure~~ of ~~Wild-type GroEL with bound Thallium ions===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_19851000}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3e76]] is a 14 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Escherichia_coli_uti89 Escherichia coli uti89]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA].~~	+

	==See Also==		==See Also==
	*[[Chaperonin\|Chaperonin]]		*[[Chaperonin\|Chaperonin]]
	*[[Heat Shock Proteins\|Heat Shock Proteins]]		*[[Heat Shock Proteins\|Heat Shock Proteins]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:019851000<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Chaperonin ATPase]]		[[Category: Chaperonin ATPase]]
	[[Category: Escherichia coli uti89]]		[[Category: Escherichia coli uti89]]

OCA at 21:30, 20 October 2012

OCA — Sat, 20 Oct 2012 21:30:20 GMT

←Older revision		Revision as of 21:30, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3e76]] is a 14 chain structure ~~of [[Chaperonin]] and [[Heat Shock Proteins]]~~ with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_uti89 Escherichia coli uti89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA].	+	[[3e76]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_uti89 Escherichia coli uti89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA].

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

OCA at 13:27, 27 July 2012

OCA — Fri, 27 Jul 2012 13:27:33 GMT

←Older revision		Revision as of 13:27, 27 July 2012
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	[[Image:3e76.png\|left\|200px]]		[[Image:3e76.png\|left\|200px]]

-	<!--
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-	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),
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	{{STRUCTURE_3e76\| PDB=3e76 \| SCENE= }}		{{STRUCTURE_3e76\| PDB=3e76 \| SCENE= }}

	===Crystal structure of Wild-type GroEL with bound Thallium ions===		===Crystal structure of Wild-type GroEL with bound Thallium ions===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19851000}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19851000 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_19851000}}		{{ABSTRACT_PUBMED_19851000}}

	==About this Structure==		==About this Structure==
-	[[3e76]] is a 14 chain structure of [[Heat Shock Proteins]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_uti89 Escherichia coli uti89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA].	+	[[3e76]] is a 14 chain structure of [[Chaperonin]] and [[Heat Shock Proteins]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_uti89 Escherichia coli uti89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA].

	==See Also==		==See Also==
-	*[[Heat Shock Proteins]]	+	*[[Chaperonin\|Chaperonin]]
		+	*[[Heat Shock Proteins\|Heat Shock Proteins]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19851000~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019851000</ref><references group="xtra"/>
	[[Category: Chaperonin ATPase]]		[[Category: Chaperonin ATPase]]
	[[Category: Escherichia coli uti89]]		[[Category: Escherichia coli uti89]]
Line 34:		Line 24:
	[[Category: Chaperone]]		[[Category: Chaperone]]
	[[Category: Chaperonin]]		[[Category: Chaperonin]]
-	[[Category: Cytoplasm]]
	[[Category: Groel]]		[[Category: Groel]]
	[[Category: Hsp60]]		[[Category: Hsp60]]
	[[Category: Nucleotide-binding]]		[[Category: Nucleotide-binding]]
	[[Category: Thallium]]		[[Category: Thallium]]

OCA: Protected "3e76" [edit=sysop:move=sysop]

OCA — Sun, 26 Dec 2010 23:32:09 GMT

Protected "3e76" [edit=sysop:move=sysop]

←Older revision

Revision as of 23:32, 26 December 2010

OCA at 23:32, 26 December 2010

OCA — Sun, 26 Dec 2010 23:32:08 GMT

←Older revision		Revision as of 23:32, 26 December 2010
Line 1:		Line 1:
-	{{Seed}}
	[[Image:3e76.png\|left\|200px]]		[[Image:3e76.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
-	~~3E76~~ is a 14 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Escherichia_coli_uti89 Escherichia coli uti89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA].	+	[[3e76]] is a 14 chain structure of [[Heat Shock Proteins]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_uti89 Escherichia coli uti89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E76 OCA].
		+
		+	==See Also==
		+	*[[Heat Shock Proteins]]

	==Reference==		==Reference==
Line 37:		Line 39:
	[[Category: Nucleotide-binding]]		[[Category: Nucleotide-binding]]
	[[Category: Thallium]]		[[Category: Thallium]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 2 08:59:28 2009''