1boq - Revision history

OCA at 05:39, 9 August 2023

OCA — Wed, 09 Aug 2023 05:39:48 GMT

←Older revision		Revision as of 05:39, 9 August 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1boq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BOQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1boq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BOQ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.1Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[https://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12]~~ </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1boq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1boq OCA], [https://pdbe.org/1boq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1boq RCSB], [https://www.ebi.ac.uk/pdbsum/1boq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1boq 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=1boq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1boq OCA], [https://pdbe.org/1boq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1boq RCSB], [https://www.ebi.ac.uk/pdbsum/1boq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1boq ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/PRLA_LYSEN PRLA_LYSEN]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Alpha-lytic endopeptidase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Lysobacter enzymogenes]]		[[Category: Lysobacter enzymogenes]]
-	[[Category: Agard~~, D A~~]]	+	[[Category: Agard DA]]
-	[[Category: Anderson~~, D E~~]]	+	[[Category: Anderson DE]]
-	[[Category: Peters~~, R J~~]]	+	[[Category: Peters RJ]]
-	[[Category: Shiau~~, A K~~]]	+	[[Category: Shiau AK]]
-	[[Category: Silen~~, J L~~]]	+	[[Category: Silen JL]]
-	[[Category: Sohl~~, J L~~]]	+	[[Category: Sohl JL]]
-	[[Category: Tang, G]]	+	[[Category: Tang G]]
-	~~[[Category: Folding mutant]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Serine protease~~]]	+

OCA at 07:01, 24 February 2021

OCA — Wed, 24 Feb 2021 07:01:26 GMT

←Older revision		Revision as of 07:01, 24 February 2021
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	<StructureSection load='1boq' size='340' side='right'caption='[[1boq]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1boq' size='340' side='right'caption='[[1boq]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1boq]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1BOQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1boq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BOQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </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=1boq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1boq OCA], [~~http~~://pdbe.org/1boq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1boq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1boq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1boq 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=1boq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1boq OCA], [https://pdbe.org/1boq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1boq RCSB], [https://www.ebi.ac.uk/pdbsum/1boq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1boq ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 09:06, 21 May 2019

OCA — Tue, 21 May 2019 09:06:02 GMT

←Older revision		Revision as of 09:06, 21 May 2019
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	==PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRITICAL IN CATALYZING THE FOLDING OF ALPHA-LYTIC PROTEASE==		==PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRITICAL IN CATALYZING THE FOLDING OF ALPHA-LYTIC PROTEASE==
-	<StructureSection load='1boq' size='340' side='right' caption='[[1boq]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='1boq' size='340' side='right'caption='[[1boq]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1boq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BOQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1boq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BOQ FirstGlance]. <br>
Line 12:		Line 12:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/1boq_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/1boq_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 29:		Line 29:

	==See Also==		==See Also==
-	*[[Alpha-lytic protease\|Alpha-lytic protease]]	+	*[[Alpha-lytic protease 3D structures\|Alpha-lytic protease 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
		+	[[Category: Large Structures]]
	[[Category: Lysobacter enzymogenes]]		[[Category: Lysobacter enzymogenes]]
	[[Category: Agard, D A]]		[[Category: Agard, D A]]

OCA at 06:03, 17 August 2017

OCA — Thu, 17 Aug 2017 06:03:11 GMT

←Older revision		Revision as of 06:03, 17 August 2017
Line 1:		Line 1:
		+
	==PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRITICAL IN CATALYZING THE FOLDING OF ALPHA-LYTIC PROTEASE==		==PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRITICAL IN CATALYZING THE FOLDING OF ALPHA-LYTIC PROTEASE==
	<StructureSection load='1boq' size='340' side='right' caption='[[1boq]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1boq' size='340' side='right' caption='[[1boq]], [[Resolution\|resolution]] 2.10Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </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=1boq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1boq OCA], [http://pdbe.org/1boq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1boq RCSB], [http://www.ebi.ac.uk/pdbsum/1boq 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=1boq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1boq OCA], [http://pdbe.org/1boq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1boq RCSB], [http://www.ebi.ac.uk/pdbsum/1boq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1boq ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 15:		Line 16:
	<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=1boq ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 10:04, 11 September 2015

OCA — Fri, 11 Sep 2015 10:04:21 GMT

←Older revision		Revision as of 10:04, 11 September 2015
Line 5:		Line 5:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </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=1boq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1boq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1boq RCSB], [http://www.ebi.ac.uk/pdbsum/1boq 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=1boq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1boq OCA], [http://pdbe.org/1boq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1boq RCSB], [http://www.ebi.ac.uk/pdbsum/1boq PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 25:		Line 25:
	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 1boq" style="background-color:#fffaf0;"></div>

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

OCA at 11:51, 22 December 2014

OCA — Mon, 22 Dec 2014 11:51:50 GMT

←Older revision		Revision as of 11:51, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1boq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BOQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1boq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BOQ FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </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=1boq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1boq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1boq RCSB], [http://www.ebi.ac.uk/pdbsum/1boq 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=1boq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1boq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1boq RCSB], [http://www.ebi.ac.uk/pdbsum/1boq PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 34:
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
	[[Category: Lysobacter enzymogenes]]		[[Category: Lysobacter enzymogenes]]
-	[[Category: Agard, D A.]]	+	[[Category: Agard, D A]]
-	[[Category: Anderson, D E.]]	+	[[Category: Anderson, D E]]
-	[[Category: Peters, R J.]]	+	[[Category: Peters, R J]]
-	[[Category: Shiau, A K.]]	+	[[Category: Shiau, A K]]
-	[[Category: Silen, J L.]]	+	[[Category: Silen, J L]]
-	[[Category: Sohl, J L.]]	+	[[Category: Sohl, J L]]
-	[[Category: Tang, G.]]	+	[[Category: Tang, G]]
	[[Category: Folding mutant]]		[[Category: Folding mutant]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Serine protease]]		[[Category: Serine protease]]

OCA at 09:36, 13 August 2014

OCA — Wed, 13 Aug 2014 09:36:04 GMT

←Older revision		Revision as of 09:36, 13 August 2014
Line 1:		Line 1:
-	[[~~Image~~:1boq.~~png\|left~~\|200px]]	+	==PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRITICAL IN CATALYZING THE FOLDING OF ALPHA-LYTIC PROTEASE==
		+	<StructureSection load='1boq' size='340' side='right' caption='[[1boq]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1boq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BOQ FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </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=1boq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1boq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1boq RCSB], [http://www.ebi.ac.uk/pdbsum/1boq 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/bo/1boq_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 ==
		+	alpha-Lytic protease is encoded with a large (166 amino acid) N-terminal pro region that is required transiently both in vivo and in vitro for the correct folding of the protease domain [Silen, J. L. , and Agard, D. A. (1989) Nature 341, 462-464; Baker, D., et al. (1992) Nature 356, 263-265]. The pro region also acts as a potent inhibitor of the mature enzyme [Baker, D., et al. (1992) Proteins: Struct.,Funct., Genet. 12, 339-344]. This inhibition is mediated through direct steric occlusion of the active site by the C-terminal residues of the pro region [Sohl, J. L., et al. (1997) Biochemistry 36, 3894-3904]. Through mutagenesis and structure-function analyses we have begun to investigate the mechanism by which the pro region acts as a single turnover catalyst to facilitate folding of the mature protease. Of central interest has been mapping the interface between the pro region and the protease and identifying interactions critical for stabilizing the rate-limiting folding transition state. Progressive C-terminal deletions of the pro region were found to have drastic effects on the rate at which the pro region folds the protease but surprisingly little effect on inhibition of protease activity. The observed kinetic data strongly support a model in which the detailed interactions between the pro region C-terminus and the protease are remarkably similar to those of known substrate/inhibitor complexes. Further, mutation of two protease residues near the active site have significant effects on stabilization of the folding transition state (kcat) or in binding to the folding intermediate (KM). Our results suggest a model for the alpha-lytic protease pro region-mediated folding reaction that may be generally applicable to other pro region-dependent folding reactions.

-	~~{{STRUCTURE_1boq\| PDB=1boq \| SCENE= }}~~	+	Pro region C-terminus:protease active site interactions are critical in catalyzing the folding of alpha-lytic protease.,Peters RJ, Shiau AK, Sohl JL, Anderson DE, Tang G, Silen JL, Agard DA Biochemistry. 1998 Sep 1;37(35):12058-67. PMID:9724517<ref>PMID:9724517</ref>

-	~~===PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRITICAL IN CATALYZING THE FOLDING OF ALPHA-LYTIC PROTEASE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_9724517}}~~	+	==See Also==
-		+	*[[Alpha-lytic protease\|Alpha-lytic protease]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1boq~~]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOQ OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:009724517<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
	[[Category: Lysobacter enzymogenes]]		[[Category: Lysobacter enzymogenes]]

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

OCA — Sun, 21 Oct 2012 20:31:21 GMT

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

←Older revision

Revision as of 20:31, 21 October 2012

OCA at 20:31, 21 October 2012

OCA — Sun, 21 Oct 2012 20:31:18 GMT

←Older revision		Revision as of 20:31, 21 October 2012
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-	{{Seed}}
	[[Image:1boq.png\|left\|200px]]		[[Image:1boq.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1boq", 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.
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	{{STRUCTURE_1boq\| PDB=1boq \| SCENE= }}		{{STRUCTURE_1boq\| PDB=1boq \| SCENE= }}

	===PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRITICAL IN CATALYZING THE FOLDING OF ALPHA-LYTIC PROTEASE===		===PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRITICAL IN CATALYZING THE FOLDING OF ALPHA-LYTIC PROTEASE===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_9724517}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 9724517 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_9724517}}		{{ABSTRACT_PUBMED_9724517}}

	==About this Structure==		==About this Structure==
-	~~1BOQ~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOQ OCA].	+	[[1boq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOQ OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~9724517~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:009724517</ref><references group="xtra"/>
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
	[[Category: Lysobacter enzymogenes]]		[[Category: Lysobacter enzymogenes]]
Line 34:		Line 22:
	[[Category: Tang, G.]]		[[Category: Tang, G.]]
	[[Category: Folding mutant]]		[[Category: Folding mutant]]
		+	[[Category: Hydrolase]]
	[[Category: Serine protease]]		[[Category: Serine protease]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 19:13:55 2009''

OCA at 17:13, 17 February 2009

OCA — Tue, 17 Feb 2009 17:13:56 GMT

←Older revision		Revision as of 17:13, 17 February 2009
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	==About this Structure==		==About this Structure==
-	1BOQ is a ~~[[Single protein]]~~ structure of sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOQ OCA].	+	1BOQ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOQ OCA].

	==Reference==		==Reference==
-	Pro region C-terminus:protease active site interactions are critical in catalyzing the folding of alpha-lytic protease., Peters RJ, Shiau AK, Sohl JL, Anderson DE, Tang G, Silen JL, Agard DA, Biochemistry. 1998 Sep 1;37(35):12058-67. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/9724517 9724517]~~	+	<ref group="xtra">PMID:9724517</ref><references group="xtra"/>
	[[Category: Alpha-lytic endopeptidase]]		[[Category: Alpha-lytic endopeptidase]]
	[[Category: Lysobacter enzymogenes]]		[[Category: Lysobacter enzymogenes]]
-	[[Category: Single protein]]
	[[Category: Agard, D A.]]		[[Category: Agard, D A.]]
	[[Category: Anderson, D E.]]		[[Category: Anderson, D E.]]
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	[[Category: Serine protease]]		[[Category: Serine protease]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Mon Jun 30~~ 19:28:~~11 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 19:13:55 2009''