3hln - Revision history

OCA at 09:58, 6 November 2024

2024-11-06T09:58:07Z

← Older revision		Revision as of 09:58, 6 November 2024
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/3hln_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/3hln_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>

OCA at 07:23, 6 September 2023

2023-09-06T07:23:48Z

← Older revision		Revision as of 07:23, 6 September 2023
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	<StructureSection load='3hln' size='340' side='right'caption='[[3hln]], [[Resolution\|resolution]] 3.20Å' scene=''>		<StructureSection load='3hln' size='340' side='right'caption='[[3hln]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3hln]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HLN FirstGlance]. <br>		<table><tr><td colspan='2'>[[3hln]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HLN 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]] 3.2Å</td></tr>
	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>b0437, clpP, JW0427, lopP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~83333 ECOLI])</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~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92]~~ </~~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=3hln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hln OCA], [https://pdbe.org/3hln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hln RCSB], [https://www.ebi.ac.uk/pdbsum/3hln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hln 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=3hln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hln OCA], [https://pdbe.org/3hln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hln RCSB], [https://www.ebi.ac.uk/pdbsum/3hln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hln ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/CLPP_ECOLI CLPP_ECOLI]] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX.		[https://www.uniprot.org/uniprot/CLPP_ECOLI CLPP_ECOLI] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	==See Also==		==See Also==
	*[[Clp protease 3D structures\|Clp protease 3D structures]]		*[[Clp protease 3D structures\|Clp protease 3D structures]]
			*[[Heat Shock Protein structures\|Heat Shock Protein structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Ecoli]]~~		[[Category: Escherichia coli K-12]]
	~~[[Category: Endopeptidase Clp~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Borg, M]]		[[Category: Borg M]]
	[[Category: Chan~~, H S~~]]		[[Category: Chan HS]]
	[[Category: Houry~~, W A~~]]		[[Category: Houry WA]]
	[[Category: Kimber~~, M S~~]]		[[Category: Kimber MS]]
	[[Category: Yu~~, A Y.H]]~~		[[Category: Yu AYH]]
	~~[[Category: Atp-binding]]~~
	~~[[Category: Disordered equatorial loop]]~~
	~~[[Category: Disulfide bond]]~~
	~~[[Category: Hydrolase]]~~
	~~[[Category: Nucleotide-binding]]~~
	~~[[Category: Protease]]~~
	~~[[Category: Serine protease]]~~
	~~[[Category: Stress response]]~~
	~~[[Category: Zymogen~~]]

OCA at 12:01, 13 October 2021

2021-10-13T12:01:24Z

← Older revision		Revision as of 12:01, 13 October 2021
Line 1:		Line 1:

	==Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds==		==Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds==
	<StructureSection load='3hln' size='340' side='right' caption='[[3hln]], [[Resolution\|resolution]] 3.20Å' scene=''>		<StructureSection load='3hln' size='340' side='right'caption='[[3hln]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3hln]] is a 28 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HLN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3HLN FirstGlance]. <br>		<table><tr><td colspan='2'>[[3hln]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HLN 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='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0437, clpP, JW0427, lopP ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0437, clpP, JW0427, lopP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </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=3hln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hln OCA], [~~http~~://pdbe.org/3hln PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3hln RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3hln PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3hln 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=3hln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hln OCA], [https://pdbe.org/3hln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hln RCSB], [https://www.ebi.ac.uk/pdbsum/3hln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hln ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/CLPP_ECOLI CLPP_ECOLI]] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX.		[[https://www.uniprot.org/uniprot/CLPP_ECOLI CLPP_ECOLI]] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	==See Also==		==See Also==
	*[[Clp ~~Protease~~\|Clp ~~Protease]]~~		*[[Clp protease 3D structures\|Clp protease 3D structures]]
	*[[Jmol/Visualizing large molecules\|Jmol/Visualizing large molecules]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Ecoli]]		[[Category: Ecoli]]
	[[Category: Endopeptidase Clp]]		[[Category: Endopeptidase Clp]]
			[[Category: Large Structures]]
	[[Category: Borg, M]]		[[Category: Borg, M]]
	[[Category: Chan, H S]]		[[Category: Chan, H S]]

OCA at 07:45, 12 December 2018

2018-12-12T07:45:59Z

← Older revision		Revision as of 07:45, 12 December 2018
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/3hln_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/3hln_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 19:13, 4 August 2016

2016-08-04T19:13:57Z

← Older revision		Revision as of 19:13, 4 August 2016
Line 1:		Line 1:

	==Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds==		==Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds==
	<StructureSection load='3hln' size='340' side='right' caption='[[3hln]], [[Resolution\|resolution]] 3.20Å' scene=''>		<StructureSection load='3hln' size='340' side='right' caption='[[3hln]], [[Resolution\|resolution]] 3.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3hln]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli Escherichia coli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HLN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HLN FirstGlance]. <br>		<table><tr><td colspan='2'>[[3hln]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HLN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HLN 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='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0437, clpP, JW0427, lopP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~562 Escherichia coli~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0437, clpP, JW0427, lopP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </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=3hln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hln OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hln RCSB], [http://www.ebi.ac.uk/pdbsum/3hln 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=3hln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hln OCA], [http://pdbe.org/3hln PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hln RCSB], [http://www.ebi.ac.uk/pdbsum/3hln PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hln ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	<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=3hln ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		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 3hln" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
			*[[Clp Protease\|Clp Protease]]
	*[[Jmol/Visualizing large molecules\|Jmol/Visualizing large molecules]]		*[[Jmol/Visualizing large molecules\|Jmol/Visualizing large molecules]]
	== References ==		== References ==
Line 35:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Ecoli]]
	[[Category: Endopeptidase Clp]]		[[Category: Endopeptidase Clp]]
	~~[[Category: Escherichia coli]]~~
	[[Category: Borg, M]]		[[Category: Borg, M]]
	[[Category: Chan, H S]]		[[Category: Chan, H S]]

OCA at 18:36, 24 December 2014

2014-12-24T18:36:53Z

← Older revision		Revision as of 18:36, 24 December 2014
Line 8:		Line 8:
	<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=3hln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hln OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hln RCSB], [http://www.ebi.ac.uk/pdbsum/3hln 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=3hln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hln OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hln RCSB], [http://www.ebi.ac.uk/pdbsum/3hln PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/CLPP_ECOLI CLPP_ECOLI]] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 28:		Line 30:

	==See Also==		==See Also==
	*[[Clp Protease\|Clp Protease]]
	*[[Jmol/Visualizing large molecules\|Jmol/Visualizing large molecules]]		*[[Jmol/Visualizing large molecules\|Jmol/Visualizing large molecules]]
	== References ==		== References ==

OCA at 06:22, 18 December 2014

2014-12-18T06:22:33Z

← Older revision		Revision as of 06:22, 18 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_3hln\| PDB=3hln \| SCENE= }}~~		==Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds==
	===Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds===		<StructureSection load='3hln' size='340' side='right' caption='[[3hln]], [[Resolution\|resolution]] 3.20Å' scene=''>
	~~{{ABSTRACT_PUBMED_20637416}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[3hln]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HLN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HLN 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>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b0437, clpP, JW0427, lopP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </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=3hln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hln OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hln RCSB], [http://www.ebi.ac.uk/pdbsum/3hln 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/hl/3hln_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 highly conserved ClpP protease consists of two heptameric rings that interact by the interdigitation of an alpha-helix beta strand handle domain motif to form a tetradecameric cylinder. We previously proposed that protease dynamics results in the temporary unstructuring of interacting pairs of handle domains, opening transient equatorial side pores that allow for peptide egress. Here, we report the structure of an Escherichia coli ClpP mutant in which each opposing pair of protomers is linked by a disulfide bond. This structure resembles the compact structures of Streptococcus pneumoniae, Mycobacterium tuberculosis, and Plasmodium falciparum ClpPs, rather than the active, extended structures that have previously been determined for E. coli ClpPs. The structural data, along with normal mode analysis, support a model whereby the ClpP cylinder switches dynamically between an active extended state required for substrate degradation and an inactive compact state allowing peptide product release.

	~~==About this~~ Structure==		Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations.,Kimber MS, Yu AY, Borg M, Leung E, Chan HS, Houry WA Structure. 2010 Jul 14;18(7):798-808. PMID:20637416<ref>PMID:20637416</ref>
	~~[[3hln]] is a 28 chain structure with sequence from [http~~:~~//en~~.~~wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.~~il/oca-bin~~/~~ocashort?id=3HLN OCA].~~
			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	==See Also==		==See Also==
	*[[Clp Protease\|Clp Protease]]		*[[Clp Protease\|Clp Protease]]
	*[[Jmol/Visualizing large molecules\|Jmol/Visualizing large molecules]]		*[[Jmol/Visualizing large molecules\|Jmol/Visualizing large molecules]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:020637416<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Endopeptidase Clp]]		[[Category: Endopeptidase Clp]]
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Borg, M.]]		[[Category: Borg, M]]
	[[Category: Chan, H S.]]		[[Category: Chan, H S]]
	[[Category: Houry, W A.]]		[[Category: Houry, W A]]
	[[Category: Kimber, M S.]]		[[Category: Kimber, M S]]
	[[Category: Yu, A Y.H.]]		[[Category: Yu, A Y.H]]
	[[Category: Atp-binding]]		[[Category: Atp-binding]]
	[[Category: Disordered equatorial loop]]		[[Category: Disordered equatorial loop]]

OCA at 10:19, 11 March 2013

2013-03-11T10:19:03Z

← Older revision		Revision as of 10:19, 11 March 2013
Line 1:		Line 1:
	~~[[Image:3hln.png\|left\|200px]]~~

	{{STRUCTURE_3hln\| PDB=3hln \| SCENE= }}		{{STRUCTURE_3hln\| PDB=3hln \| SCENE= }}

	===Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds===		===Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds===

	{{ABSTRACT_PUBMED_20637416}}		{{ABSTRACT_PUBMED_20637416}}

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

2012-10-20T08:02:19Z

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

← Older revision	Revision as of 08:02, 20 October 2012
(No difference)

OCA at 08:02, 20 October 2012

2012-10-20T08:02:16Z

← Older revision		Revision as of 08:02, 20 October 2012
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	~~{{Seed}}~~		[[Image:3hln.png\|left\|200px]]
	[[Image:3hln.~~jpg~~\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_3hln", 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.~~
	~~-->~~
	{{STRUCTURE_3hln\| PDB=3hln \| SCENE= }}		{{STRUCTURE_3hln\| PDB=3hln \| SCENE= }}

	===Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds===		===Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_20637416}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 20637416 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_20637416}}		{{ABSTRACT_PUBMED_20637416}}

	==About this Structure==		==About this Structure==
	~~3HLN~~ is a 28 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/~~Escherichia_coli_k-12~~ Escherichia coli ~~k-12~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HLN OCA].		[[3hln]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HLN OCA].

			==See Also==
			*[[Clp Protease\|Clp Protease]]
			*[[Jmol/Visualizing large molecules\|Jmol/Visualizing large molecules]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~20637416~~</ref><references group="xtra"/>		<ref group="xtra">PMID:020637416</ref><references group="xtra"/>
	[[Category: Endopeptidase Clp]]		[[Category: Endopeptidase Clp]]
	[[Category: Escherichia coli ~~k-12~~]]		[[Category: Escherichia coli]]
	[[Category: Borg, M.]]		[[Category: Borg, M.]]
	[[Category: Chan, H S.]]		[[Category: Chan, H S.]]
Line 40:		Line 32:
	[[Category: Stress response]]		[[Category: Stress response]]
	[[Category: Zymogen]]		[[Category: Zymogen]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 28 12:35:42 2010''~~