1z0g - Revision history

OCA at 09:01, 14 February 2024

2024-02-14T09:01:43Z

←Older revision		Revision as of 09:01, 14 February 2024
Line 3:		Line 3:
	<StructureSection load='1z0g' size='340' side='right'caption='[[1z0g]], [[Resolution\|resolution]] 2.27Å' scene=''>		<StructureSection load='1z0g' size='340' side='right'caption='[[1z0g]], [[Resolution\|resolution]] 2.27Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1z0g]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Arcfl Arcfl~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z0G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1z0g]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z0G 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;'>[[1z0b\|1z0b]]~~, [[~~1z0c~~\|~~1z0c~~]]~~, [[1z0e\|1z0e]], [[1z0v\|1z0v]], [[1z0t\|1z0t]], [[1z0w\|1z0w]]</div></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.27Å</td></tr>
-	~~<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en~~.~~wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </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=1z0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0g OCA], [https://pdbe.org/1z0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z0g RCSB], [https://www.ebi.ac.uk/pdbsum/1z0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z0g 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=1z0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0g OCA], [https://pdbe.org/1z0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z0g RCSB], [https://www.ebi.ac.uk/pdbsum/1z0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z0g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/LONB_ARCFU LONB_ARCFU]] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).	+	[https://www.uniprot.org/uniprot/LONB_ARCFU LONB_ARCFU] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 19:
	</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=1z0g 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=1z0g ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The atomic-resolution crystal structure of the proteolytic domain (P-domain, residues 415-621) of Archaeoglobus fulgidus B-type Lon protease (wtAfLonB) and the structures of several mutants have revealed significant differences in the conformation of the active-site residues when compared to other known Lon P-domains, despite the conservation of the overall fold. The catalytic Ser509 is facing the solvent and is distant from Lys552, the other member of the catalytic dyad. Instead, the adjacent Asp508 forms an ion pair with the catalytic lysine residue. Glu506, an analog of the putative third catalytic residue from a related Methanococcus jannaschii LonB, also faces the solvent and does not interact with the catalytic dyad. We have established that full-length wtAfLonB is proteolytically active in an ATP-dependent manner. The loss of enzymatic activity of the S509A mutant confirms the functional significance of this residue, while retention of considerable level of activity by the D508A and E506A mutants rules out their critical involvement in catalysis. In contrast to the full-length enzymes, all individually purified P-domains (wild-type and mutants) were inactive, and the mutations had no influence on the active-site structure. These findings raise the possibility that, although isolated proteolytic domains of both AfLonB and E.coli LonA are able to assemble into expected functional hexamers, the presence of the other domains, as well as substrate binding, may be needed to stabilize the productive conformation of their active sites. Thus, the observed conformational variability may reflect the differences in the stability of active-site structures for the proteolytic counterparts of single-chain Lon versus independently folded proteolytic subunits of two-chain AAA+ proteases.
-
-	Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteases.,Botos I, Melnikov EE, Cherry S, Kozlov S, Makhovskaya OV, Tropea JE, Gustchina A, Rotanova TV, Wlodawer A J Mol Biol. 2005 Aug 5;351(1):144-57. PMID:16002085<ref>PMID:16002085</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1z0g" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Arcfl]]~~	+	[[Category: Archaeoglobus fulgidus]]
-	~~[[Category: Endopeptidase La~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Botos, I]]	+	[[Category: Botos I]]
-	[[Category: Cherry, S]]	+	[[Category: Cherry S]]
-	[[Category: Gustchina, A]]	+	[[Category: Gustchina A]]
-	[[Category: Kozlov, S]]	+	[[Category: Kozlov S]]
-	[[Category: Makhovskaya~~, O V~~]]	+	[[Category: Makhovskaya OV]]
-	[[Category: Melnikov~~, E E~~]]	+	[[Category: Melnikov EE]]
-	[[Category: Rotanova~~, T V~~]]	+	[[Category: Rotanova TV]]
-	[[Category: Tropea~~, J E~~]]	+	[[Category: Tropea JE]]
-	[[Category: Wlodawer, A]]	+	[[Category: Wlodawer A]]
-	~~[[Category: Atp-dependent protease]]~~	+
-	~~[[Category: B-type lonss']]~~	+
-	~~[[Category: Catalytic ser-lys dyad]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 06:07, 28 April 2021

2021-04-28T06:07:32Z

←Older revision		Revision as of 06:07, 28 April 2021
Line 3:		Line 3:
	<StructureSection load='1z0g' size='340' side='right'caption='[[1z0g]], [[Resolution\|resolution]] 2.27Å' scene=''>		<StructureSection load='1z0g' size='340' side='right'caption='[[1z0g]], [[Resolution\|resolution]] 2.27Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1z0g]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0G OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1Z0G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1z0g]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z0G FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z0b\|1z0b]], [[1z0c\|1z0c]], [[1z0e\|1z0e]], [[1z0v\|1z0v]], [[1z0t\|1z0t]], [[1z0w\|1z0w]]</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;'>[[1z0b\|1z0b]], [[1z0c\|1z0c]], [[1z0e\|1z0e]], [[1z0v\|1z0v]], [[1z0t\|1z0t]], [[1z0w\|1z0w]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </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_La Endopeptidase La], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </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=1z0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0g OCA], [~~http~~://pdbe.org/1z0g PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1z0g RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1z0g PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1z0g 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=1z0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0g OCA], [https://pdbe.org/1z0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z0g RCSB], [https://www.ebi.ac.uk/pdbsum/1z0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z0g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/LONB_ARCFU LONB_ARCFU]] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).	+	[[https://www.uniprot.org/uniprot/LONB_ARCFU LONB_ARCFU]] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 09:06, 24 July 2019

2019-07-24T09:06:41Z

←Older revision		Revision as of 09:06, 24 July 2019
Line 1:		Line 1:

	==Crystal Structure of A. fulgidus Lon proteolytic domain==		==Crystal Structure of A. fulgidus Lon proteolytic domain==
-	<StructureSection load='1z0g' size='340' side='right' caption='[[1z0g]], [[Resolution\|resolution]] 2.27Å' scene=''>	+	<StructureSection load='1z0g' size='340' side='right'caption='[[1z0g]], [[Resolution\|resolution]] 2.27Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1z0g]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z0G FirstGlance]. <br>		<table><tr><td colspan='2'>[[1z0g]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z0G FirstGlance]. <br>
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/z0/1z0g_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z0/1z0g_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 35:		Line 35:
	[[Category: Arcfl]]		[[Category: Arcfl]]
	[[Category: Endopeptidase La]]		[[Category: Endopeptidase La]]
		+	[[Category: Large Structures]]
	[[Category: Botos, I]]		[[Category: Botos, I]]
	[[Category: Cherry, S]]		[[Category: Cherry, S]]
Line 45:		Line 46:
	[[Category: Wlodawer, A]]		[[Category: Wlodawer, A]]
	[[Category: Atp-dependent protease]]		[[Category: Atp-dependent protease]]
-	[[Category: B-type ~~lons~~']]	+	[[Category: B-type lonss']]
	[[Category: Catalytic ser-lys dyad]]		[[Category: Catalytic ser-lys dyad]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 10:40, 12 October 2017

2017-10-12T10:40:57Z

←Older revision		Revision as of 10:40, 12 October 2017
Line 1:		Line 1:
		+
	==Crystal Structure of A. fulgidus Lon proteolytic domain==		==Crystal Structure of A. fulgidus Lon proteolytic domain==
	<StructureSection load='1z0g' size='340' side='right' caption='[[1z0g]], [[Resolution\|resolution]] 2.27Å' scene=''>		<StructureSection load='1z0g' size='340' side='right' caption='[[1z0g]], [[Resolution\|resolution]] 2.27Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z0b\|1z0b]], [[1z0c\|1z0c]], [[1z0e\|1z0e]], [[1z0v\|1z0v]], [[1z0t\|1z0t]], [[1z0w\|1z0w]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z0b\|1z0b]], [[1z0c\|1z0c]], [[1z0e\|1z0e]], [[1z0v\|1z0v]], [[1z0t\|1z0t]], [[1z0w\|1z0w]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </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_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </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=1z0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0g OCA], [http://pdbe.org/1z0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z0g RCSB], [http://www.ebi.ac.uk/pdbsum/1z0g 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=1z0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0g OCA], [http://pdbe.org/1z0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z0g RCSB], [http://www.ebi.ac.uk/pdbsum/1z0g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z0g 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=1z0g ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 00:33, 12 September 2015

2015-09-12T00:33:19Z

←Older revision		Revision as of 00:33, 12 September 2015
Line 2:		Line 2:
	<StructureSection load='1z0g' size='340' side='right' caption='[[1z0g]], [[Resolution\|resolution]] 2.27Å' scene=''>		<StructureSection load='1z0g' size='340' side='right' caption='[[1z0g]], [[Resolution\|resolution]] 2.27Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1z0g]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Archaeoglobus_fulgidus Archaeoglobus fulgidus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z0G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1z0g]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z0G FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z0b\|1z0b]], [[1z0c\|1z0c]], [[1z0e\|1z0e]], [[1z0v\|1z0v]], [[1z0t\|1z0t]], [[1z0w\|1z0w]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z0b\|1z0b]], [[1z0c\|1z0c]], [[1z0e\|1z0e]], [[1z0v\|1z0v]], [[1z0t\|1z0t]], [[1z0w\|1z0w]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </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_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </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=1z0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1z0g RCSB], [http://www.ebi.ac.uk/pdbsum/1z0g 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=1z0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0g OCA], [http://pdbe.org/1z0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z0g RCSB], [http://www.ebi.ac.uk/pdbsum/1z0g PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~LONH_ARCFU LONH_ARCFU~~]] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).	+	[[http://www.uniprot.org/uniprot/LONB_ARCFU LONB_ARCFU]] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 27:		Line 27:
	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 1z0g" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Archaeoglobus fulgidus~~]]	+	[[Category: Arcfl]]
	[[Category: Endopeptidase La]]		[[Category: Endopeptidase La]]
	[[Category: Botos, I]]		[[Category: Botos, I]]

OCA at 21:28, 25 December 2014

2014-12-25T21:28:26Z

←Older revision		Revision as of 21:28, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1z0g]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z0G FirstGlance]. <br>		<table><tr><td colspan='2'>[[1z0g]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z0G FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z0b\|1z0b]], [[1z0c\|1z0c]], [[1z0e\|1z0e]], [[1z0v\|1z0v]], [[1z0t\|1z0t]], [[1z0w\|1z0w]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z0b\|1z0b]], [[1z0c\|1z0c]], [[1z0e\|1z0e]], [[1z0v\|1z0v]], [[1z0t\|1z0t]], [[1z0w\|1z0w]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </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_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </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=1z0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1z0g RCSB], [http://www.ebi.ac.uk/pdbsum/1z0g 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=1z0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1z0g RCSB], [http://www.ebi.ac.uk/pdbsum/1z0g PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/LONH_ARCFU LONH_ARCFU]] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Degrades polypeptides processively (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 33:
	[[Category: Archaeoglobus fulgidus]]		[[Category: Archaeoglobus fulgidus]]
	[[Category: Endopeptidase La]]		[[Category: Endopeptidase La]]
-	[[Category: Botos, I.]]	+	[[Category: Botos, I]]
-	[[Category: Cherry, S.]]	+	[[Category: Cherry, S]]
-	[[Category: Gustchina, A.]]	+	[[Category: Gustchina, A]]
-	[[Category: Kozlov, S.]]	+	[[Category: Kozlov, S]]
-	[[Category: Makhovskaya, O V.]]	+	[[Category: Makhovskaya, O V]]
-	[[Category: Melnikov, E E.]]	+	[[Category: Melnikov, E E]]
-	[[Category: Rotanova, T V.]]	+	[[Category: Rotanova, T V]]
-	[[Category: Tropea, J E.]]	+	[[Category: Tropea, J E]]
-	[[Category: Wlodawer, A.]]	+	[[Category: Wlodawer, A]]
	[[Category: Atp-dependent protease]]		[[Category: Atp-dependent protease]]
	[[Category: B-type lons']]		[[Category: B-type lons']]
	[[Category: Catalytic ser-lys dyad]]		[[Category: Catalytic ser-lys dyad]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 20:52, 29 September 2014

2014-09-29T20:52:55Z

←Older revision		Revision as of 20:52, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1z0g.~~png~~\|~~left~~\|200px]]	+	==Crystal Structure of A. fulgidus Lon proteolytic domain==
		+	<StructureSection load='1z0g' size='340' side='right' caption='[[1z0g]], [[Resolution\|resolution]] 2.27Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1z0g]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z0G FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z0b\|1z0b]], [[1z0c\|1z0c]], [[1z0e\|1z0e]], [[1z0v\|1z0v]], [[1z0t\|1z0t]], [[1z0w\|1z0w]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </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=1z0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1z0g RCSB], [http://www.ebi.ac.uk/pdbsum/1z0g 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/z0/1z0g_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 atomic-resolution crystal structure of the proteolytic domain (P-domain, residues 415-621) of Archaeoglobus fulgidus B-type Lon protease (wtAfLonB) and the structures of several mutants have revealed significant differences in the conformation of the active-site residues when compared to other known Lon P-domains, despite the conservation of the overall fold. The catalytic Ser509 is facing the solvent and is distant from Lys552, the other member of the catalytic dyad. Instead, the adjacent Asp508 forms an ion pair with the catalytic lysine residue. Glu506, an analog of the putative third catalytic residue from a related Methanococcus jannaschii LonB, also faces the solvent and does not interact with the catalytic dyad. We have established that full-length wtAfLonB is proteolytically active in an ATP-dependent manner. The loss of enzymatic activity of the S509A mutant confirms the functional significance of this residue, while retention of considerable level of activity by the D508A and E506A mutants rules out their critical involvement in catalysis. In contrast to the full-length enzymes, all individually purified P-domains (wild-type and mutants) were inactive, and the mutations had no influence on the active-site structure. These findings raise the possibility that, although isolated proteolytic domains of both AfLonB and E.coli LonA are able to assemble into expected functional hexamers, the presence of the other domains, as well as substrate binding, may be needed to stabilize the productive conformation of their active sites. Thus, the observed conformational variability may reflect the differences in the stability of active-site structures for the proteolytic counterparts of single-chain Lon versus independently folded proteolytic subunits of two-chain AAA+ proteases.

-	~~{{STRUCTURE_1z0g\| PDB=1z0g \| SCENE= }}~~	+	Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteases.,Botos I, Melnikov EE, Cherry S, Kozlov S, Makhovskaya OV, Tropea JE, Gustchina A, Rotanova TV, Wlodawer A J Mol Biol. 2005 Aug 5;351(1):144-57. PMID:16002085<ref>PMID:16002085</ref>

-	~~===Crystal Structure~~ of A. ~~fulgidus Lon proteolytic domain===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_16002085}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1z0g]] is a 6 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org~~/~~wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0G OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:016002085<~~/~~ref~~><~~ref group="xtra">PMID:015983420</ref><references group="xtra"~~/>	+
	[[Category: Archaeoglobus fulgidus]]		[[Category: Archaeoglobus fulgidus]]
	[[Category: Endopeptidase La]]		[[Category: Endopeptidase La]]

OCA at 12:25, 23 January 2013

2013-01-23T12:25:36Z

←Older revision		Revision as of 12:25, 23 January 2013
Line 1:		Line 1:
	[[Image:1z0g.png\|left\|200px]]		[[Image:1z0g.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1z0g", 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_1z0g\| PDB=1z0g \| SCENE= }}		{{STRUCTURE_1z0g\| PDB=1z0g \| SCENE= }}

	===Crystal Structure of A. fulgidus Lon proteolytic domain===		===Crystal Structure of A. fulgidus Lon proteolytic domain===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_16002085}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 16002085 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_16002085}}		{{ABSTRACT_PUBMED_16002085}}

Line 22:		Line 11:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~16002085~~</ref><ref group="xtra">PMID:~~15983420~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:016002085</ref><ref group="xtra">PMID:015983420</ref><references group="xtra"/>
	[[Category: Archaeoglobus fulgidus]]		[[Category: Archaeoglobus fulgidus]]
	[[Category: Endopeptidase La]]		[[Category: Endopeptidase La]]

OCA: Protected "1z0g" [edit=sysop:move=sysop]

2011-03-14T20:00:00Z

Protected "1z0g" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:00, 14 March 2011

OCA at 19:59, 14 March 2011

2011-03-14T19:59:58Z

←Older revision		Revision as of 19:59, 14 March 2011
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1z0g.png\|left\|200px]]		[[Image:1z0g.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
-	~~1Z0G~~ is a 6 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0G OCA].	+	[[1z0g]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0G OCA].

	==Reference==		==Reference==
Line 38:		Line 37:
	[[Category: B-type lons']]		[[Category: B-type lons']]
	[[Category: Catalytic ser-lys dyad]]		[[Category: Catalytic ser-lys dyad]]
-		+	[[Category: Hydrolase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Wed Feb 18 08:10:56 2009''~~	+