2pre - Revision history

OCA at 05:26, 17 October 2024

2024-10-17T05:26:36Z

← Older revision		Revision as of 05:26, 17 October 2024
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/2pre_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/2pre_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>

OCA at 11:07, 30 August 2023

2023-08-30T11:07:23Z

← Older revision		Revision as of 11:07, 30 August 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2pre]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Tabernaemontana_divaricata Tabernaemontana divaricata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PRE FirstGlance]. <br>		<table><tr><td colspan='2'>[[2pre]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Tabernaemontana_divaricata Tabernaemontana divaricata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PRE FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=E64:N~~-[N-[~~1-HYDROXYCARBOXYETHYL-CARBONYL~~]~~LEUCYLAMINO-BUTYL~~]~~-GUANIDINE'>E64</scene>, <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]] 2.7Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;'>~~[[~~1o0e\|1o0e~~]], ~~[[2pns\|2pns]]~~</~~div~~></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <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=2pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pre OCA], [https://pdbe.org/2pre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pre RCSB], [https://www.ebi.ac.uk/pdbsum/2pre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pre 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=2pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pre OCA], [https://pdbe.org/2pre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pre RCSB], [https://www.ebi.ac.uk/pdbsum/2pre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pre ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[https://www.uniprot.org/uniprot/ERVC2_TABDI ERVC2_TABDI] Cysteine proteinase (PubMed:18167146). Hydrolyzes denatured natural substrates such as casein, hemoglobin, azoalbumin and azocasein with a high specific activity (By similarity). Has little or no activity against synthetic substrates (By similarity).[UniProtKB:P83654]<ref>PMID:18167146</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Tabernaemontana divaricata]]		[[Category: Tabernaemontana divaricata]]
	[[Category: Biswas, S]]		[[Category: Biswas S]]
	[[Category: Chakrabarti, C]]		[[Category: Chakrabarti C]]
	[[Category: Dattagupta~~, J K~~]]		[[Category: Dattagupta JK]]
	[[Category: Ghosh, R]]		[[Category: Ghosh R]]
	~~[[Category: Ervatamin]]~~
	~~[[Category: Hydrolase]]~~
	~~[[Category: Papain-like fold]]~~
	~~[[Category: Plant cysteine protease]]~~
	~~[[Category: Protease-inhibitor complex~~]]

OCA at 07:47, 9 March 2022

2022-03-09T07:47:08Z

← Older revision		Revision as of 07:47, 9 March 2022
Line 3:		Line 3:
	<StructureSection load='2pre' size='340' side='right'caption='[[2pre]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='2pre' size='340' side='right'caption='[[2pre]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2pre]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Tabernaemontana_divaricata Tabernaemontana divaricata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2PRE FirstGlance]. <br>		<table><tr><td colspan='2'>[[2pre]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Tabernaemontana_divaricata Tabernaemontana divaricata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PRE FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <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=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0e\|1o0e]], [[2pns\|2pns]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1o0e\|1o0e]], [[2pns\|2pns]]</div></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pre OCA], [~~http~~://pdbe.org/2pre PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2pre RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2pre PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2pre 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=2pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pre OCA], [https://pdbe.org/2pre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pre RCSB], [https://www.ebi.ac.uk/pdbsum/2pre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pre ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 06:57, 3 June 2020

2020-06-03T06:57:18Z

← Older revision		Revision as of 06:57, 3 June 2020
Line 1:		Line 1:

	==Crystal structure of plant cysteine protease Ervatamin-C complexed with irreversible inhibitor E-64 at 2.7 A resolution==		==Crystal structure of plant cysteine protease Ervatamin-C complexed with irreversible inhibitor E-64 at 2.7 A resolution==
	<StructureSection load='2pre' size='340' side='right' caption='[[2pre]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='2pre' size='340' side='right'caption='[[2pre]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2pre]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Tabernaemontana_divaricata Tabernaemontana divaricata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRE OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2PRE FirstGlance]. <br>		<table><tr><td colspan='2'>[[2pre]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Tabernaemontana_divaricata Tabernaemontana divaricata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2PRE FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <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=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0e\|1o0e]], [[2pns\|2pns]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0e\|1o0e]], [[2pns\|2pns]]</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=2pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pre OCA], [http://pdbe.org/2pre PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pre RCSB], [http://www.ebi.ac.uk/pdbsum/2pre PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pre ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pre OCA], [http://pdbe.org/2pre PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pre RCSB], [http://www.ebi.ac.uk/pdbsum/2pre PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pre ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Large Structures]]
	[[Category: Tabernaemontana divaricata]]		[[Category: Tabernaemontana divaricata]]
	[[Category: Biswas, S]]		[[Category: Biswas, S]]

OCA at 08:39, 29 August 2018

2018-08-29T08:39:39Z

← Older revision		Revision as of 08:39, 29 August 2018
Line 1:		Line 1:

	==Crystal structure of plant cysteine protease Ervatamin-C complexed with irreversible inhibitor E-64 at 2.7 A resolution==		==Crystal structure of plant cysteine protease Ervatamin-C complexed with irreversible inhibitor E-64 at 2.7 A resolution==
	<StructureSection load='2pre' size='340' side='right' caption='[[2pre]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='2pre' size='340' side='right' caption='[[2pre]], [[Resolution\|resolution]] 2.70Å' scene=''>
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <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=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0e\|1o0e]], [[2pns\|2pns]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0e\|1o0e]], [[2pns\|2pns]]</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=2pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pre OCA], [http://pdbe.org/2pre PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pre RCSB], [http://www.ebi.ac.uk/pdbsum/2pre 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=2pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pre OCA], [http://pdbe.org/2pre PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pre RCSB], [http://www.ebi.ac.uk/pdbsum/2pre PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pre ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/2pre_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/2pre_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 23:05, 7 February 2016

2016-02-07T23:05:10Z

← Older revision		Revision as of 23:05, 7 February 2016
Line 15:		Line 15:
	<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=2pre ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 05:41, 10 September 2015

2015-09-10T05:41:28Z

← Older revision		Revision as of 05:41, 10 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=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <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=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0e\|1o0e]], [[2pns\|2pns]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0e\|1o0e]], [[2pns\|2pns]]</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=2pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pre OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pre RCSB], [http://www.ebi.ac.uk/pdbsum/2pre 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=2pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pre OCA], [http://pdbe.org/2pre PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pre RCSB], [http://www.ebi.ac.uk/pdbsum/2pre PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	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 2pre" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:46, 19 January 2015

2015-01-19T16:46:42Z

← Older revision		Revision as of 16:46, 19 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2pre]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Tabernaemontana_divaricata Tabernaemontana divaricata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PRE FirstGlance]. <br>		<table><tr><td colspan='2'>[[2pre]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Tabernaemontana_divaricata Tabernaemontana divaricata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PRE FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <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=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0e\|1o0e]], [[2pns\|2pns]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0e\|1o0e]], [[2pns\|2pns]]</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=2pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pre OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pre RCSB], [http://www.ebi.ac.uk/pdbsum/2pre 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=2pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pre OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pre RCSB], [http://www.ebi.ac.uk/pdbsum/2pre 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 30:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Tabernaemontana divaricata]]		[[Category: Tabernaemontana divaricata]]
	[[Category: Biswas, S.]]		[[Category: Biswas, S]]
	[[Category: Chakrabarti, C.]]		[[Category: Chakrabarti, C]]
	[[Category: Dattagupta, J K.]]		[[Category: Dattagupta, J K]]
	[[Category: Ghosh, R.]]		[[Category: Ghosh, R]]
	[[Category: Ervatamin]]		[[Category: Ervatamin]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 19:27, 30 September 2014

2014-09-30T19:27:31Z

← Older revision		Revision as of 19:27, 30 September 2014
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	[[Image:~~2pre~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal structure of plant cysteine protease Ervatamin-C complexed with irreversible inhibitor E-64 at 2.7 A resolution==
			<StructureSection load='2pre' size='340' side='right' caption='[[2pre]], [[Resolution\|resolution]] 2.70Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2pre]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Tabernaemontana_divaricata Tabernaemontana divaricata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PRE FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1o0e\|1o0e]], [[2pns\|2pns]]</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=2pre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pre OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pre RCSB], [http://www.ebi.ac.uk/pdbsum/2pre 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/pr/2pre_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 ==
			Multiple proteases of the same family are quite often present in the same species in biological systems. These multiple proteases, despite having high homology in their primary and tertiary structures, show deviations in properties such as stability, activity, and specificity. It is of interest, therefore, to compare the structures of these multiple proteases in a single species to identify the structural changes, if any, that may be responsible for such deviations. Ervatamin-A, ervatamin-B and ervatamin-C are three such papain-like cysteine proteases found in the latex of the tropical plant Ervatamia coronaria, and are known not only for their high stability over a wide range of temperature and pH, but also for variations in activity and specificity among themselves and among other members of the family. Here we report the crystal structures of ervatamin-A and ervatamin-C, complexed with an irreversible inhibitor 1-[l-N-(trans-epoxysuccinyl)leucyl]amino-4-guanidinobutane (E-64), together with enzyme kinetics and molecular dynamic simulation studies. A comparison of these results with the earlier structures helps in a correlation of the structural features with the corresponding functional properties. The specificity constants (k(cat)/K(m)) for the ervatamins indicate that all of these enzymes have specificity for a branched hydrophobic residue at the P2 position of the peptide substrates, with different degrees of efficiency. A single amino acid change, as compared to ervatamin-C, in the S2 pocket of ervatamin-A (Ala67-->Tyr) results in a 57-fold increase in its k(cat)/K(m) value for a substrate having a Val at the P2 position. Our studies indicate a higher enzymatic activity of ervatamin-A, which has been subsequently explained at the molecular level from the three-dimensional structure of the enzyme and in the context of its helix polarizibility and active site plasticity.

	~~{{STRUCTURE_2pre\| PDB=2pre \| SCENE= }}~~		Structural insights into the substrate specificity and activity of ervatamins, the papain-like cysteine proteases from a tropical plant, Ervatamia coronaria.,Ghosh R, Chakraborty S, Chakrabarti C, Dattagupta JK, Biswas S FEBS J. 2008 Feb;275(3):421-34. Epub 2007 Dec 19. PMID:18167146<ref>PMID:18167146</ref>

	~~===Crystal structure~~ of ~~plant cysteine protease Ervatamin-C complexed with irreversible inhibitor E-64 at 2~~.~~7 A resolution===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_18167146}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[2pre]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org~~/~~wiki/Tabernaemontana_divaricata Tabernaemontana divaricata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRE OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:018167146<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Tabernaemontana divaricata]]		[[Category: Tabernaemontana divaricata]]
	[[Category: Biswas, S.]]		[[Category: Biswas, S.]]

OCA: Protected "2pre" [edit=sysop:move=sysop]

2013-01-07T11:48:18Z

Protected "2pre" [edit=sysop:move=sysop]

← Older revision	Revision as of 11:48, 7 January 2013
(No difference)