2ku1 - Revision history

OCA at 09:41, 22 May 2024

2024-05-22T09:41:34Z

←Older revision		Revision as of 09:41, 22 May 2024
Line 1:		Line 1:

	==Dynamic Regulation of Archaeal Proteasome Gate Opening as Studied by TROSY-NMR==		==Dynamic Regulation of Archaeal Proteasome Gate Opening as Studied by TROSY-NMR==
-	<StructureSection load='2ku1' size='340' side='right'caption='[[2ku1~~]], [[NMR_Ensembles_of_Models \| 30 NMR models~~]]' scene=''>	+	<StructureSection load='2ku1' size='340' side='right'caption='[[2ku1]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ku1]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KU1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ku1]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KU1 FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1pma\|1pma]], [[1ya7\|1ya7]], [[2ku2\|2ku2]]</div></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">psmA, Ta1288 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </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=2ku1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku1 OCA], [https://pdbe.org/2ku1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ku1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ku1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ku1 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=2ku1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku1 OCA], [https://pdbe.org/2ku1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ku1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ku1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ku1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PSA_THEAC PSA_THEAC]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.<ref>PMID:8999862</ref>	+	[https://www.uniprot.org/uniprot/PSA_THEAC PSA_THEAC] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.<ref>PMID:8999862</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 38:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Proteasome endopeptidase complex~~]]	+	[[Category: Thermoplasma acidophilum]]
-	[[Category: Kay~~, L E~~]]	+	[[Category: Kay LE]]
-	[[Category: Religa~~, T L~~]]	+	[[Category: Religa TL]]
-	[[Category: Sprangers, R]]	+	[[Category: Sprangers R]]
-	~~[[Category: Cytoplasm]]~~	+
-	~~[[Category: Gating residue]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Protease]]~~	+
-	~~[[Category: Proteasome]]~~	+
-	~~[[Category: Proteolysis]]~~	+
-	~~[[Category: Threonine protease~~]]	+

OCA at 07:32, 14 April 2021

2021-04-14T07:32:08Z

←Older revision		Revision as of 07:32, 14 April 2021
Line 1:		Line 1:
-	~~{{Large structure}}~~	+
	==Dynamic Regulation of Archaeal Proteasome Gate Opening as Studied by TROSY-NMR==		==Dynamic Regulation of Archaeal Proteasome Gate Opening as Studied by TROSY-NMR==
-	<StructureSection load='2ku1' size='340' side='right' caption='[[2ku1]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>	+	<StructureSection load='2ku1' size='340' side='right'caption='[[2ku1]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ku1]] is a 7 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KU1 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2KU1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ku1]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KU1 FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pma\|1pma]], [[1ya7\|1ya7]], [[2ku2\|2ku2]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pma\|1pma]], [[1ya7\|1ya7]], [[2ku2\|2ku2]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">psmA, Ta1288 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">psmA, Ta1288 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </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=2ku1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku1 OCA], [~~http~~://pdbe.org/2ku1 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2ku1 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2ku1 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2ku1 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=2ku1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku1 OCA], [https://pdbe.org/2ku1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ku1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ku1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ku1 ProSAT]</span></td></tr>
	</table>		</table>
-	{{Large structure}}
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PSA_THEAC PSA_THEAC]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.<ref>PMID:8999862</ref>	+	[[https://www.uniprot.org/uniprot/PSA_THEAC PSA_THEAC]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.<ref>PMID:8999862</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 32:

	==See Also==		==See Also==
-	*[[Proteasome\|Proteasome]]	+	*[[Proteasome 3D structures\|Proteasome 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Proteasome endopeptidase complex]]		[[Category: Proteasome endopeptidase complex]]
	[[Category: Kay, L E]]		[[Category: Kay, L E]]

OCA at 08:15, 25 July 2018

2018-07-25T08:15:12Z

←Older revision		Revision as of 08:15, 25 July 2018
Line 1:		Line 1:
		+	{{Large structure}}
	==Dynamic Regulation of Archaeal Proteasome Gate Opening as Studied by TROSY-NMR==		==Dynamic Regulation of Archaeal Proteasome Gate Opening as Studied by TROSY-NMR==
	<StructureSection load='2ku1' size='340' side='right' caption='[[2ku1]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>		<StructureSection load='2ku1' size='340' side='right' caption='[[2ku1]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">psmA, Ta1288 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">psmA, Ta1288 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </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=2ku1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku1 OCA], [http://pdbe.org/2ku1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ku1 RCSB], [http://www.ebi.ac.uk/pdbsum/2ku1 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=2ku1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku1 OCA], [http://pdbe.org/2ku1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ku1 RCSB], [http://www.ebi.ac.uk/pdbsum/2ku1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ku1 ProSAT]</span></td></tr>
	</table>		</table>
	{{Large structure}}		{{Large structure}}
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ku/2ku1_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ku/2ku1_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>
	</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=2ku1 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 41:		Line 42:
	[[Category: Religa, T L]]		[[Category: Religa, T L]]
	[[Category: Sprangers, R]]		[[Category: Sprangers, R]]
		+	[[Category: Cytoplasm]]
	[[Category: Gating residue]]		[[Category: Gating residue]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 02:22, 12 September 2015

2015-09-12T02:22:59Z

←Older revision		Revision as of 02:22, 12 September 2015
Line 2:		Line 2:
	<StructureSection load='2ku1' size='340' side='right' caption='[[2ku1]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>		<StructureSection load='2ku1' size='340' side='right' caption='[[2ku1]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ku1]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Thermoplasma_acidophilum Thermoplasma acidophilum~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KU1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KU1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ku1]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KU1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KU1 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pma\|1pma]], [[1ya7\|1ya7]], [[2ku2\|2ku2]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pma\|1pma]], [[1ya7\|1ya7]], [[2ku2\|2ku2]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">psmA, Ta1288 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma ~~acidophilum~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">psmA, Ta1288 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </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=2ku1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ku1 RCSB], [http://www.ebi.ac.uk/pdbsum/2ku1 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=2ku1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku1 OCA], [http://pdbe.org/2ku1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ku1 RCSB], [http://www.ebi.ac.uk/pdbsum/2ku1 PDBsum]</span></td></tr>
	</table>		</table>
		+	{{Large structure}}
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~PSMA_THEAC PSMA_THEAC~~]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.<ref>PMID:8999862</ref>	+	[[http://www.uniprot.org/uniprot/PSA_THEAC PSA_THEAC]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.<ref>PMID:8999862</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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 2ku1" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Proteasome endopeptidase complex]]		[[Category: Proteasome endopeptidase complex]]
-	[[Category: Thermoplasma acidophilum]]
	[[Category: Kay, L E]]		[[Category: Kay, L E]]
	[[Category: Religa, T L]]		[[Category: Religa, T L]]

OCA at 22:39, 25 December 2014

2014-12-25T22:39:12Z

←Older revision		Revision as of 22:39, 25 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=2ku1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ku1 RCSB], [http://www.ebi.ac.uk/pdbsum/2ku1 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=2ku1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ku1 RCSB], [http://www.ebi.ac.uk/pdbsum/2ku1 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PSMA_THEAC PSMA_THEAC]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.<ref>PMID:8999862</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 13:46, 17 December 2014

2014-12-17T13:46:12Z

←Older revision		Revision as of 13:46, 17 December 2014
Line 1:		Line 1:
-	~~{{Large structure}}~~	+	==Dynamic Regulation of Archaeal Proteasome Gate Opening as Studied by TROSY-NMR==
-	~~{{STRUCTURE_2ku1\| PDB=2ku1 \| SCENE= }}~~	+	<StructureSection load='2ku1' size='340' side='right' caption='[[2ku1]], [[NMR_Ensembles_of_Models \| 30 NMR models]]' scene=''>
-	===Dynamic Regulation of Archaeal Proteasome Gate Opening as Studied by TROSY-NMR===	+	== Structural highlights ==
-	~~{{ABSTRACT_PUBMED_20360109}}~~	+	<table><tr><td colspan='2'>[[2ku1]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KU1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KU1 FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pma\|1pma]], [[1ya7\|1ya7]], [[2ku2\|2ku2]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">psmA, Ta1288 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </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=2ku1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ku1 RCSB], [http://www.ebi.ac.uk/pdbsum/2ku1 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/ku/2ku1_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 proteasome catalyzes the majority of protein degradation in the cell and plays an integral role in cellular homeostasis. Control over proteolysis by the 20S core-particle (CP) proteasome is achieved by gated access of substrate; thus, an understanding of the molecular mechanism by which these gates regulate substrate entry is critical. We used methyl-transverse relaxation optimized nuclear magnetic resonance spectroscopy to show that the amino-terminal residues that compose the gates of the alpha subunits of the Thermoplasma acidophilum proteasome are highly dynamic over a broad spectrum of time scales and that gating termini are in conformations that extend either well inside (closed gate) or outside (open gate) of the antechamber. Interconversion between these conformers on a time scale of seconds leads to a dynamic regulation of 20S CP proteolysis activity.

-	~~==About this Structure==~~	+	Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR.,Religa TL, Sprangers R, Kay LE Science. 2010 Apr 2;328(5974):98-102. PMID:20360109<ref>PMID:20360109</ref>
-	~~[[2ku1]] is a 7 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]~~. ~~Full experimental information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=2KU1 OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Proteasome\|Proteasome]]		*[[Proteasome\|Proteasome]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:020360109<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Proteasome endopeptidase complex]]		[[Category: Proteasome endopeptidase complex]]
	[[Category: Thermoplasma acidophilum]]		[[Category: Thermoplasma acidophilum]]
-	[[Category: Kay, L E.]]	+	[[Category: Kay, L E]]
-	[[Category: Religa, T L.]]	+	[[Category: Religa, T L]]
-	[[Category: Sprangers, R.]]	+	[[Category: Sprangers, R]]
	[[Category: Gating residue]]		[[Category: Gating residue]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 08:14, 11 March 2013

2013-03-11T08:14:15Z

←Older revision		Revision as of 08:14, 11 March 2013
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	{{Large structure}}		{{Large structure}}
-	[[Image:2ku1.png\|left\|200px]]
-
	{{STRUCTURE_2ku1\| PDB=2ku1 \| SCENE= }}		{{STRUCTURE_2ku1\| PDB=2ku1 \| SCENE= }}
-
	===Dynamic Regulation of Archaeal Proteasome Gate Opening as Studied by TROSY-NMR===		===Dynamic Regulation of Archaeal Proteasome Gate Opening as Studied by TROSY-NMR===
-
	{{ABSTRACT_PUBMED_20360109}}		{{ABSTRACT_PUBMED_20360109}}

OCA at 22:29, 20 October 2012

2012-10-20T22:29:01Z

←Older revision		Revision as of 22:29, 20 October 2012
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	==About this Structure==		==About this Structure==
-	[[2ku1]] is a 7 chain structure ~~of [[Proteasome]]~~ with sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KU1 OCA].	+	[[2ku1]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KU1 OCA].

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

OCA at 16:28, 27 July 2012

2012-07-27T16:28:04Z

←Older revision		Revision as of 16:28, 27 July 2012
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	[[Image:2ku1.png\|left\|200px]]		[[Image:2ku1.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2ku1", 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_2ku1\| PDB=2ku1 \| SCENE= }}		{{STRUCTURE_2ku1\| PDB=2ku1 \| SCENE= }}

	===Dynamic Regulation of Archaeal Proteasome Gate Opening as Studied by TROSY-NMR===		===Dynamic Regulation of Archaeal Proteasome Gate Opening as Studied by TROSY-NMR===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20360109}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20360109 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_20360109}}		{{ABSTRACT_PUBMED_20360109}}

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

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20360109~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020360109</ref><references group="xtra"/>
	[[Category: Proteasome endopeptidase complex]]		[[Category: Proteasome endopeptidase complex]]
	[[Category: Thermoplasma acidophilum]]		[[Category: Thermoplasma acidophilum]]
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	[[Category: Religa, T L.]]		[[Category: Religa, T L.]]
	[[Category: Sprangers, R.]]		[[Category: Sprangers, R.]]
-	[[Category: Cytoplasm]]
	[[Category: Gating residue]]		[[Category: Gating residue]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 04:06, 11 January 2011

2011-01-11T04:06:56Z

←Older revision		Revision as of 04:06, 11 January 2011
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		+	{{Large structure}}
	[[Image:2ku1.png\|left\|200px]]		[[Image:2ku1.png\|left\|200px]]