2pkp - Revision history

OCA at 09:00, 25 October 2023

2023-10-25T09:00:57Z

←Older revision		Revision as of 09:00, 25 October 2023
Line 3:		Line 3:
	<StructureSection load='2pkp' size='340' side='right'caption='[[2pkp]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2pkp' size='340' side='right'caption='[[2pkp]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2pkp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Metja Metja~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PKP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2pkp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PKP FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>~~, ~~<scene name='pdbligand=ZN:ZINC+ION'>ZN</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='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>aksE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~243232 METJA])</td~~><~~/tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Methanogen_homoaconitase Methanogen homoaconitase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.114 4.2.1.114]~~ </~~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=2pkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkp OCA], [https://pdbe.org/2pkp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pkp RCSB], [https://www.ebi.ac.uk/pdbsum/2pkp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pkp ProSAT], [https://www.topsan.org/Proteins/RSGI/2pkp TOPSAN]</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=2pkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkp OCA], [https://pdbe.org/2pkp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pkp RCSB], [https://www.ebi.ac.uk/pdbsum/2pkp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pkp ProSAT], [https://www.topsan.org/Proteins/RSGI/2pkp TOPSAN]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/HACB_METJA HACB_METJA]] Hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are part of the biosynthesis pathway of coenzyme B. Can also catalyze the hydration of maleate to (R)-malate, and that of cis-aconitate. Can not catalyze the hydration of citraconate and the dehydration of (S)-homocitrate, citramalate, 2-isopropylmalate, 3-isopropylmalate, citrate or threo-DL-isocitrate.<ref>PMID:17449626</ref> <ref>PMID:18765671</ref> <ref>PMID:20170198</ref>	+	[https://www.uniprot.org/uniprot/HACB_METJA HACB_METJA] Hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are part of the biosynthesis pathway of coenzyme B. Can also catalyze the hydration of maleate to (R)-malate, and that of cis-aconitate. Can not catalyze the hydration of citraconate and the dehydration of (S)-homocitrate, citramalate, 2-isopropylmalate, 3-isopropylmalate, citrate or threo-DL-isocitrate.<ref>PMID:17449626</ref> <ref>PMID:18765671</ref> <ref>PMID:20170198</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 40:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Methanogen homoaconitase]]~~	+	[[Category: Methanocaldococcus jannaschii DSM 2661]]
-	~~[[Category: Metja~~]]	+	[[Category: Agari Y]]
-	[[Category: Agari, Y]]	+	[[Category: Ebihara A]]
-	[[Category: Ebihara, A]]	+	[[Category: Gayathri DR]]
-	[[Category: Gayathri~~, D R~~]]	+	[[Category: Jeyakanthan J]]
-	[[Category: Jeyakanthan, J]]	+	[[Category: Kuramitsu S]]
-	[[Category: Kuramitsu, S]]	+	[[Category: Shinkai A]]
-	~~[[Category: Structural genomic~~]]	+	[[Category: Shiro Y]]
-	[[Category: Shinkai, A]]	+	[[Category: Velmurugan D]]
-	[[Category: Shiro, Y]]	+	[[Category: Yokoyama S]]
-	[[Category: Velmurugan, D]]	+
-	[[Category: Yokoyama, S]]	+
-	~~[[Category: Amino-acid biosynthesis]]~~	+
-	~~[[Category: Beta barrel]]~~	+
-	~~[[Category: Leucine biosynthesis]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: National project on protein structural and functional analyse]]~~	+
-	~~[[Category: Nppsfa]]~~	+
-	~~[[Category: Rsgi~~]]	+

OCA at 15:26, 17 June 2021

2021-06-17T15:26:18Z

←Older revision		Revision as of 15:26, 17 June 2021
Line 1:		Line 1:

	==Crystal structure of 3-isopropylmalate dehydratase (leuD)from Methhanocaldococcus Jannaschii DSM2661 (MJ1271)==		==Crystal structure of 3-isopropylmalate dehydratase (leuD)from Methhanocaldococcus Jannaschii DSM2661 (MJ1271)==
-	<StructureSection load='2pkp' size='340' side='right' caption='[[2pkp]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='2pkp' size='340' side='right'caption='[[2pkp]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2pkp]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Metja Metja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2PKP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2pkp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Metja Metja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PKP FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aksE ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 METJA])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aksE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 METJA])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Methanogen_homoaconitase Methanogen homoaconitase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.114 4.2.1.114] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methanogen_homoaconitase Methanogen homoaconitase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.114 4.2.1.114] </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=2pkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkp OCA], [~~http~~://pdbe.org/2pkp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2pkp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2pkp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2pkp ProSAT], [~~http~~://www.topsan.org/Proteins/RSGI/2pkp TOPSAN]</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=2pkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkp OCA], [https://pdbe.org/2pkp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pkp RCSB], [https://www.ebi.ac.uk/pdbsum/2pkp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pkp ProSAT], [https://www.topsan.org/Proteins/RSGI/2pkp TOPSAN]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/HACB_METJA HACB_METJA]] Hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are part of the biosynthesis pathway of coenzyme B. Can also catalyze the hydration of maleate to (R)-malate, and that of cis-aconitate. Can not catalyze the hydration of citraconate and the dehydration of (S)-homocitrate, citramalate, 2-isopropylmalate, 3-isopropylmalate, citrate or threo-DL-isocitrate.<ref>PMID:17449626</ref> <ref>PMID:18765671</ref> <ref>PMID:20170198</ref>	+	[[https://www.uniprot.org/uniprot/HACB_METJA HACB_METJA]] Hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are part of the biosynthesis pathway of coenzyme B. Can also catalyze the hydration of maleate to (R)-malate, and that of cis-aconitate. Can not catalyze the hydration of citraconate and the dehydration of (S)-homocitrate, citramalate, 2-isopropylmalate, 3-isopropylmalate, citrate or threo-DL-isocitrate.<ref>PMID:17449626</ref> <ref>PMID:18765671</ref> <ref>PMID:20170198</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 39:		Line 39:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Methanogen homoaconitase]]		[[Category: Methanogen homoaconitase]]
	[[Category: Metja]]		[[Category: Metja]]

OCA at 08:25, 29 August 2018

2018-08-29T08:25:21Z

←Older revision		Revision as of 08:25, 29 August 2018
Line 1:		Line 1:
		+
	==Crystal structure of 3-isopropylmalate dehydratase (leuD)from Methhanocaldococcus Jannaschii DSM2661 (MJ1271)==		==Crystal structure of 3-isopropylmalate dehydratase (leuD)from Methhanocaldococcus Jannaschii DSM2661 (MJ1271)==
	<StructureSection load='2pkp' size='340' side='right' caption='[[2pkp]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2pkp' size='340' side='right' caption='[[2pkp]], [[Resolution\|resolution]] 2.10Å' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aksE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 METJA])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aksE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 METJA])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methanogen_homoaconitase Methanogen homoaconitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.114 4.2.1.114] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methanogen_homoaconitase Methanogen homoaconitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.114 4.2.1.114] </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=2pkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkp OCA], [http://pdbe.org/2pkp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pkp RCSB], [http://www.ebi.ac.uk/pdbsum/2pkp PDBsum], [http://www.topsan.org/Proteins/RSGI/2pkp TOPSAN]</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=2pkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkp OCA], [http://pdbe.org/2pkp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pkp RCSB], [http://www.ebi.ac.uk/pdbsum/2pkp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pkp ProSAT], [http://www.topsan.org/Proteins/RSGI/2pkp TOPSAN]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pk/2pkp_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pk/2pkp_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=2pkp ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 33:		Line 34:
	*[[Homoaconitase\|Homoaconitase]]		*[[Homoaconitase\|Homoaconitase]]
	*[[Isopropylmalate dehydrogenase\|Isopropylmalate dehydrogenase]]		*[[Isopropylmalate dehydrogenase\|Isopropylmalate dehydrogenase]]
		+	*[[Isopropylmalate isomerase\|Isopropylmalate isomerase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:09, 12 September 2015

2015-09-12T02:09:04Z

←Older revision		Revision as of 02:09, 12 September 2015
Line 2:		Line 2:
	<StructureSection load='2pkp' size='340' side='right' caption='[[2pkp]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2pkp' size='340' side='right' caption='[[2pkp]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2pkp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Methanocaldococcus_jannaschii Methanocaldococcus jannaschii~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PKP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2pkp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Metja Metja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PKP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aksE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=~~2190 Methanocaldococcus jannaschii~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aksE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 METJA])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methanogen_homoaconitase Methanogen homoaconitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.114 4.2.1.114] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methanogen_homoaconitase Methanogen homoaconitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.114 4.2.1.114] </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=2pkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pkp RCSB], [http://www.ebi.ac.uk/pdbsum/2pkp PDBsum], [http://www.topsan.org/Proteins/RSGI/2pkp TOPSAN]</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=2pkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkp OCA], [http://pdbe.org/2pkp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pkp RCSB], [http://www.ebi.ac.uk/pdbsum/2pkp PDBsum], [http://www.topsan.org/Proteins/RSGI/2pkp TOPSAN]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	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 2pkp" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Methanocaldococcus jannaschii]]
	[[Category: Methanogen homoaconitase]]		[[Category: Methanogen homoaconitase]]
		+	[[Category: Metja]]
	[[Category: Agari, Y]]		[[Category: Agari, Y]]
	[[Category: Ebihara, A]]		[[Category: Ebihara, A]]

OCA at 22:29, 25 December 2014

2014-12-25T22:29:32Z

←Older revision		Revision as of 22:29, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2pkp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PKP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2pkp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PKP FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aksE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aksE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methanogen_homoaconitase Methanogen homoaconitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.114 4.2.1.114] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methanogen_homoaconitase Methanogen homoaconitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.114 4.2.1.114] </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=2pkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pkp RCSB], [http://www.ebi.ac.uk/pdbsum/2pkp PDBsum], [http://www.topsan.org/Proteins/RSGI/2pkp TOPSAN]</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=2pkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pkp RCSB], [http://www.ebi.ac.uk/pdbsum/2pkp PDBsum], [http://www.topsan.org/Proteins/RSGI/2pkp TOPSAN]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HACB_METJA HACB_METJA]] Hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are part of the biosynthesis pathway of coenzyme B. Can also catalyze the hydration of maleate to (R)-malate, and that of cis-aconitate. Can not catalyze the hydration of citraconate and the dehydration of (S)-homocitrate, citramalate, 2-isopropylmalate, 3-isopropylmalate, citrate or threo-DL-isocitrate.<ref>PMID:17449626</ref> <ref>PMID:18765671</ref> <ref>PMID:20170198</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 38:
	[[Category: Methanocaldococcus jannaschii]]		[[Category: Methanocaldococcus jannaschii]]
	[[Category: Methanogen homoaconitase]]		[[Category: Methanogen homoaconitase]]
-	[[Category: Agari, Y.]]	+	[[Category: Agari, Y]]
-	[[Category: Ebihara, A.]]	+	[[Category: Ebihara, A]]
-	[[Category: Gayathri, D R.]]	+	[[Category: Gayathri, D R]]
-	[[Category: Jeyakanthan, J.]]	+	[[Category: Jeyakanthan, J]]
-	[[Category: Kuramitsu, S.]]	+	[[Category: Kuramitsu, S]]
-	[[Category: ~~RSGI, RIKEN~~ Structural ~~Genomics/Proteomics Initiative.~~]]	+	[[Category: Structural genomic]]
-	[[Category: Shinkai, A.]]	+	[[Category: Shinkai, A]]
-	[[Category: Shiro, Y.]]	+	[[Category: Shiro, Y]]
-	[[Category: Velmurugan, D.]]	+	[[Category: Velmurugan, D]]
-	[[Category: Yokoyama, S.]]	+	[[Category: Yokoyama, S]]
	[[Category: Amino-acid biosynthesis]]		[[Category: Amino-acid biosynthesis]]
	[[Category: Beta barrel]]		[[Category: Beta barrel]]
Line 52:		Line 54:
	[[Category: National project on protein structural and functional analyse]]		[[Category: National project on protein structural and functional analyse]]
	[[Category: Nppsfa]]		[[Category: Nppsfa]]
-	[[Category: Riken structural genomics/proteomics initiative]]
	[[Category: Rsgi]]		[[Category: Rsgi]]
-	[[Category: Structural genomic]]

OCA at 09:40, 29 September 2014

2014-09-29T09:40:36Z

←Older revision		Revision as of 09:40, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2pkp.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of 3-isopropylmalate dehydratase (leuD)from Methhanocaldococcus Jannaschii DSM2661 (MJ1271)==
		+	<StructureSection load='2pkp' size='340' side='right' caption='[[2pkp]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2pkp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PKP FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">aksE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methanogen_homoaconitase Methanogen homoaconitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.114 4.2.1.114] </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=2pkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pkp RCSB], [http://www.ebi.ac.uk/pdbsum/2pkp PDBsum], [http://www.topsan.org/Proteins/RSGI/2pkp TOPSAN]</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/pk/2pkp_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 aconitase family of hydro-lyase enzymes includes three classes of proteins that catalyze the isomerization of alpha-hydroxy acids to beta-hydroxy acids. Besides aconitase, isopropylmalate isomerase (IPMI) proteins specifically catalyze the isomerization of alpha,beta-dicarboxylates with hydrophobic gamma-chain groups, and homoaconitase (HACN) proteins catalyze the isomerization of tricarboxylates with variable chain length gamma-carboxylate groups. These enzymes' stereospecific hydro-lyase activities make them attractive catalysts to produce diastereomers from unsaturated precursors. However, sequence similarity and convergent evolution among these proteins lead to widespread misannotation and uncertainty about gene function. To find the substrate specificity determinants of homologous IPMI and HACN proteins from Methanocaldococcus jannaschii, the small-subunit HACN protein (MJ1271) was crystallized for X-ray diffraction. The structural model showed characteristic residues in a flexible loop region between alpha2 and alpha3 that distinguish HACN from IPMI and aconitase proteins. Site-directed mutagenesis of MJ1271 produced loop-region variant proteins that were reconstituted with wild-type MJ1003 large-subunit protein. The heteromers formed promiscuous hydro-lyases with reduced activity but broader substrate specificity. Both R26K and R26V variants formed relatively efficient IPMI enzymes, while the T27A variant had uniformly lower specificity constants for both IPMI and HACN substrates. The R26V T27Y variant resembles the MJ1277 IPMI small subunit in its flexible loop sequence but demonstrated the broad substrate specificity of the R26V variant. These mutations may reverse the evolution of HACN activity from an ancestral IPMI gene, demonstrating the evolutionary potential for promiscuity in hydro-lyase enzymes. Understanding these specificity determinants enables the functional reannotation of paralogous HACN and IPMI genes in numerous genome sequences. These structural and kinetic results will help to engineer new stereospecific hydro-lyase enzymes for chemoenzymatic syntheses.

-	~~{{STRUCTURE_2pkp\| PDB=2pkp \| SCENE= }}~~	+	Substrate specificity determinants of the methanogen homoaconitase enzyme: structure and function of the small subunit.,Jeyakanthan J, Drevland RM, Gayathri DR, Velmurugan D, Shinkai A, Kuramitsu S, Yokoyama S, Graham DE Biochemistry. 2010 Mar 30;49(12):2687-96. PMID:20170198<ref>PMID:20170198</ref>

-	~~===Crystal structure~~ of ~~3-isopropylmalate dehydratase (leuD)from Methhanocaldococcus Jannaschii DSM2661 (MJ1271)===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_20170198}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2pkp]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA].~~	+

	==See Also==		==See Also==
	*[[Homoaconitase\|Homoaconitase]]		*[[Homoaconitase\|Homoaconitase]]
	*[[Isopropylmalate dehydrogenase\|Isopropylmalate dehydrogenase]]		*[[Isopropylmalate dehydrogenase\|Isopropylmalate dehydrogenase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:020170198<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Methanocaldococcus jannaschii]]		[[Category: Methanocaldococcus jannaschii]]
	[[Category: Methanogen homoaconitase]]		[[Category: Methanogen homoaconitase]]

OCA at 22:23, 20 October 2012

2012-10-20T22:23:48Z

←Older revision		Revision as of 22:23, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2pkp]] is a 1 chain structure ~~of [[Homoaconitase]] and [[Isopropylmalate dehydrogenase]]~~ with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA].	+	[[2pkp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA].

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

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

2012-07-27T16:09:40Z

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

←Older revision

Revision as of 16:09, 27 July 2012

OCA at 16:09, 27 July 2012

2012-07-27T16:09:39Z

←Older revision		Revision as of 16:09, 27 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2pkp.png\|left\|200px]]		[[Image:2pkp.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2pkp", 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_2pkp\| PDB=2pkp \| SCENE= }}		{{STRUCTURE_2pkp\| PDB=2pkp \| SCENE= }}

	===Crystal structure of 3-isopropylmalate dehydratase (leuD)from Methhanocaldococcus Jannaschii DSM2661 (MJ1271)===		===Crystal structure of 3-isopropylmalate dehydratase (leuD)from Methhanocaldococcus Jannaschii DSM2661 (MJ1271)===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20170198}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20170198 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_20170198}}		{{ABSTRACT_PUBMED_20170198}}

	==About this Structure==		==About this Structure==
-	~~2PKP~~ is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA].	+	[[2pkp]] is a 1 chain structure of [[Homoaconitase]] and [[Isopropylmalate dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA].
		+
		+	==See Also==
		+	*[[Homoaconitase\|Homoaconitase]]
		+	*[[Isopropylmalate dehydrogenase\|Isopropylmalate dehydrogenase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20170198~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020170198</ref><references group="xtra"/>
	[[Category: Methanocaldococcus jannaschii]]		[[Category: Methanocaldococcus jannaschii]]
	[[Category: Methanogen homoaconitase]]		[[Category: Methanogen homoaconitase]]
Line 45:		Line 37:
	[[Category: Rsgi]]		[[Category: Rsgi]]
	[[Category: Structural genomic]]		[[Category: Structural genomic]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 7 10:13:38 2010''

OCA at 07:13, 7 April 2010

2010-04-07T07:13:38Z

←Older revision		Revision as of 07:13, 7 April 2010
Line 12:		Line 12:
	===Crystal structure of 3-isopropylmalate dehydratase (leuD)from Methhanocaldococcus Jannaschii DSM2661 (MJ1271)===		===Crystal structure of 3-isopropylmalate dehydratase (leuD)from Methhanocaldococcus Jannaschii DSM2661 (MJ1271)===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_20170198}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 20170198 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_20170198}}

	==About this Structure==		==About this Structure==
-	2PKP is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA].	+	2PKP is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA].
-	~~[[Category~~: ~~3-isopropylmalate dehydratase]]~~	+
		+	==Reference==
		+	<ref group="xtra">PMID:20170198</ref><references group="xtra"/>
	[[Category: Methanocaldococcus jannaschii]]		[[Category: Methanocaldococcus jannaschii]]
		+	[[Category: Methanogen homoaconitase]]
	[[Category: Agari, Y.]]		[[Category: Agari, Y.]]
	[[Category: Ebihara, A.]]		[[Category: Ebihara, A.]]
-	[[Category: Gayathri, D.]]	+	[[Category: Gayathri, D R.]]
	[[Category: Jeyakanthan, J.]]		[[Category: Jeyakanthan, J.]]
	[[Category: Kuramitsu, S.]]		[[Category: Kuramitsu, S.]]
Line 37:		Line 46:
	[[Category: Structural genomic]]		[[Category: Structural genomic]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun Nov 16 18~~:05:~~10 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 7 10:13:38 2010''