2v68 - Revision history

OCA at 15:07, 13 December 2023

OCA — Wed, 13 Dec 2023 15:07:51 GMT

←Older revision		Revision as of 15:07, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='2v68' size='340' side='right'caption='[[2v68]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2v68' size='340' side='right'caption='[[2v68]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2v68]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Chlre Chlre~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V68 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2v68]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V68 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CAP:2~~-~~CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=EDO:1~~,2~~-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.3Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~HYP~~:4-~~HYDROXYPROLINE~~'>~~HYP~~</scene>, <scene name='pdbligand=~~KCX~~:~~LYSINE+NZ~~-~~CARBOXYLIC+ACID~~'>~~KCX~~</scene>, <scene name='pdbligand=~~MME~~:N-~~METHYL+METHIONINE~~'>~~MME~~</scene>, <scene name='pdbligand=~~SMC~~:S-~~METHYLCYSTEINE~~'>~~SMC~~</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MME:N-METHYL+METHIONINE'>MME</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b~~></td><~~td class~~=~~"sblockDat"><div style~~=~~'overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[1uw9\|1uw9]], [[1uzh\|1uzh]], [[1gk8\|1gk8]], [[1uwa\|1uwa]], [[1ir2\|1ir2]], [[1uzd\|1uzd]], [[2v63\|2v63]], [[2v67\|2v67]], [[2v69\|2v69]], [[2v6a\|2v6a]]~~</~~div~~><~~/td></tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39]~~ </~~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=2v68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v68 OCA], [https://pdbe.org/2v68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v68 RCSB], [https://www.ebi.ac.uk/pdbsum/2v68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v68 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=2v68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v68 OCA], [https://pdbe.org/2v68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v68 RCSB], [https://www.ebi.ac.uk/pdbsum/2v68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v68 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/RBL_CHLRE RBL_CHLRE]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338] [[https://www.uniprot.org/uniprot/RBS1_CHLRE RBS1_CHLRE]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.	+	[https://www.uniprot.org/uniprot/RBL_CHLRE RBL_CHLRE] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]
	== 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: ~~Chlre~~]]	+	[[Category: Chlamydomonas reinhardtii]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Ribulose-bisphosphate carboxylase]]~~	+	[[Category: Andersson I]]
-	[[Category: Andersson, I]]	+	[[Category: Karkehabadi S]]
-	[[Category: Karkehabadi, S]]	+	[[Category: Satagopan S]]
-	[[Category: Satagopan, S]]	+	[[Category: Spreitzer RJ]]
-	[[Category: Spreitzer~~, R J~~]]	+	[[Category: Taylor TC]]
-	[[Category: Taylor~~, T C]]~~	+
-	~~[[Category: Acetylation]]~~	+
-	~~[[Category: Calvin cycle]]~~	+
-	~~[[Category: Carbon dioxide fixation]]~~	+
-	~~[[Category: Chloroplast]]~~	+
-	~~[[Category: Co2/o2 specificity]]~~	+
-	~~[[Category: Hydroxylation]]~~	+
-	~~[[Category: Large subunit loop 6 mutation]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Magnesium]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Methylation]]~~	+
-	~~[[Category: Monooxygenase]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Photorespiration]]~~	+
-	~~[[Category: Photosynthesis]]~~	+
-	~~[[Category: Plastid]]~~	+
-	~~[[Category: Rubisco]]~~	+
-	~~[[Category: Transit peptide~~]]	+

OCA at 20:58, 20 October 2021

OCA — Wed, 20 Oct 2021 20:58:03 GMT

←Older revision		Revision as of 20:58, 20 October 2021
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	<StructureSection load='2v68' size='340' side='right'caption='[[2v68]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2v68' size='340' side='right'caption='[[2v68]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2v68]] is a 16 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2V68 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2v68]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V68 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MME:N-METHYL+METHIONINE'>MME</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MME:N-METHYL+METHIONINE'>MME</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1uw9\|1uw9]], [[1uzh\|1uzh]], [[1gk8\|1gk8]], [[1uwa\|1uwa]], [[1ir2\|1ir2]], [[1uzd\|1uzd]], [[2v63\|2v63]], [[2v67\|2v67]], [[2v69\|2v69]], [[2v6a\|2v6a]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1uw9\|1uw9]], [[1uzh\|1uzh]], [[1gk8\|1gk8]], [[1uwa\|1uwa]], [[1ir2\|1ir2]], [[1uzd\|1uzd]], [[2v63\|2v63]], [[2v67\|2v67]], [[2v69\|2v69]], [[2v6a\|2v6a]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </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=2v68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v68 OCA], [~~http~~://pdbe.org/2v68 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2v68 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2v68 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2v68 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=2v68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v68 OCA], [https://pdbe.org/2v68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v68 RCSB], [https://www.ebi.ac.uk/pdbsum/2v68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v68 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/RBL_CHLRE RBL_CHLRE]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338] [[~~http~~://www.uniprot.org/uniprot/RBS1_CHLRE RBS1_CHLRE]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.	+	[[https://www.uniprot.org/uniprot/RBL_CHLRE RBL_CHLRE]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338] [[https://www.uniprot.org/uniprot/RBS1_CHLRE RBS1_CHLRE]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	==See Also==		==See Also==
-	*[[RuBisCO\|RuBisCO]]	+	*[[RuBisCO 3D structures\|RuBisCO 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:54, 18 December 2019

OCA — Wed, 18 Dec 2019 13:54:08 GMT

←Older revision		Revision as of 13:54, 18 December 2019
Line 1:		Line 1:

	==Crystal structure of Chlamydomonas reinhardtii Rubisco with large- subunit mutations V331A, T342I==		==Crystal structure of Chlamydomonas reinhardtii Rubisco with large- subunit mutations V331A, T342I==
-	<StructureSection load='2v68' size='340' side='right' caption='[[2v68]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='2v68' size='340' side='right'caption='[[2v68]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2v68]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V68 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2v68]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V68 FirstGlance]. <br>
Line 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 2v68" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2v68" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[RuBisCO\|RuBisCO]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Chlre]]		[[Category: Chlre]]
		+	[[Category: Large Structures]]
	[[Category: Ribulose-bisphosphate carboxylase]]		[[Category: Ribulose-bisphosphate carboxylase]]
	[[Category: Andersson, I]]		[[Category: Andersson, I]]

OCA at 07:26, 17 January 2018

OCA — Wed, 17 Jan 2018 07:26:14 GMT

←Older revision		Revision as of 07:26, 17 January 2018
Line 1:		Line 1:
-	==~~CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH LARGE~~-~~SUBUNIT MUTATIONS~~ V331A, T342I==	+
		+	==Crystal structure of Chlamydomonas reinhardtii Rubisco with large- subunit mutations V331A, T342I==
	<StructureSection load='2v68' size='340' side='right' caption='[[2v68]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2v68' size='340' side='right' caption='[[2v68]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 7:		Line 8:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1uw9\|1uw9]], [[1uzh\|1uzh]], [[1gk8\|1gk8]], [[1uwa\|1uwa]], [[1ir2\|1ir2]], [[1uzd\|1uzd]], [[2v63\|2v63]], [[2v67\|2v67]], [[2v69\|2v69]], [[2v6a\|2v6a]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1uw9\|1uw9]], [[1uzh\|1uzh]], [[1gk8\|1gk8]], [[1uwa\|1uwa]], [[1ir2\|1ir2]], [[1uzd\|1uzd]], [[2v63\|2v63]], [[2v67\|2v67]], [[2v69\|2v69]], [[2v6a\|2v6a]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </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=2v68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v68 OCA], [http://pdbe.org/2v68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v68 RCSB], [http://www.ebi.ac.uk/pdbsum/2v68 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=2v68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v68 OCA], [http://pdbe.org/2v68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v68 RCSB], [http://www.ebi.ac.uk/pdbsum/2v68 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v68 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v6/2v68_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v6/2v68_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 30:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 2v68" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2v68" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[RuBisCO\|RuBisCO]]
	== References ==		== References ==
	<references/>		<references/>
Line 44:		Line 42:
	[[Category: Spreitzer, R J]]		[[Category: Spreitzer, R J]]
	[[Category: Taylor, T C]]		[[Category: Taylor, T C]]
		+	[[Category: Acetylation]]
	[[Category: Calvin cycle]]		[[Category: Calvin cycle]]
	[[Category: Carbon dioxide fixation]]		[[Category: Carbon dioxide fixation]]
Line 58:		Line 57:
	[[Category: Photorespiration]]		[[Category: Photorespiration]]
	[[Category: Photosynthesis]]		[[Category: Photosynthesis]]
		+	[[Category: Plastid]]
	[[Category: Rubisco]]		[[Category: Rubisco]]
	[[Category: Transit peptide]]		[[Category: Transit peptide]]

OCA at 13:02, 9 February 2016

OCA — Tue, 09 Feb 2016 13:02:51 GMT

←Older revision		Revision as of 13:02, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='2v68' size='340' side='right' caption='[[2v68]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2v68' size='340' side='right' caption='[[2v68]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2v68]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Chlamydomonas_reinhardtii Chlamydomonas reinhardtii~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V68 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2v68]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V68 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MME:N-METHYL+METHIONINE'>MME</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MME:N-METHYL+METHIONINE'>MME</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1uw9\|1uw9]], [[1uzh\|1uzh]], [[1gk8\|1gk8]], [[1uwa\|1uwa]], [[1ir2\|1ir2]], [[1uzd\|1uzd]], [[2v63\|2v63]], [[2v67\|2v67]], [[2v69\|2v69]], [[2v6a\|2v6a]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1uw9\|1uw9]], [[1uzh\|1uzh]], [[1gk8\|1gk8]], [[1uwa\|1uwa]], [[1ir2\|1ir2]], [[1uzd\|1uzd]], [[2v63\|2v63]], [[2v67\|2v67]], [[2v69\|2v69]], [[2v6a\|2v6a]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </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=2v68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v68 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v68 RCSB], [http://www.ebi.ac.uk/pdbsum/2v68 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=2v68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v68 OCA], [http://pdbe.org/2v68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v68 RCSB], [http://www.ebi.ac.uk/pdbsum/2v68 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 19:
	<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=2v68 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 29:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2v68" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Chlamydomonas reinhardtii~~]]	+	[[Category: Chlre]]
	[[Category: Ribulose-bisphosphate carboxylase]]		[[Category: Ribulose-bisphosphate carboxylase]]
	[[Category: Andersson, I]]		[[Category: Andersson, I]]

OCA at 06:59, 25 December 2014

OCA — Thu, 25 Dec 2014 06:59:17 GMT

←Older revision		Revision as of 06:59, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2v68]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V68 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2v68]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V68 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MME:N-METHYL+METHIONINE'>MME</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MME:N-METHYL+METHIONINE'>MME</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1uw9\|1uw9]], [[1uzh\|1uzh]], [[1gk8\|1gk8]], [[1uwa\|1uwa]], [[1ir2\|1ir2]], [[1uzd\|1uzd]], [[2v63\|2v63]], [[2v67\|2v67]], [[2v69\|2v69]], [[2v6a\|2v6a]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1uw9\|1uw9]], [[1uzh\|1uzh]], [[1gk8\|1gk8]], [[1uwa\|1uwa]], [[1ir2\|1ir2]], [[1uzd\|1uzd]], [[2v63\|2v63]], [[2v67\|2v67]], [[2v69\|2v69]], [[2v6a\|2v6a]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </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=2v68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v68 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v68 RCSB], [http://www.ebi.ac.uk/pdbsum/2v68 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=2v68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v68 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v68 RCSB], [http://www.ebi.ac.uk/pdbsum/2v68 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RBL_CHLRE RBL_CHLRE]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338] [[http://www.uniprot.org/uniprot/RBS1_CHLRE RBS1_CHLRE]] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 38:
	[[Category: Chlamydomonas reinhardtii]]		[[Category: Chlamydomonas reinhardtii]]
	[[Category: Ribulose-bisphosphate carboxylase]]		[[Category: Ribulose-bisphosphate carboxylase]]
-	[[Category: Andersson, I.]]	+	[[Category: Andersson, I]]
-	[[Category: Karkehabadi, S.]]	+	[[Category: Karkehabadi, S]]
-	[[Category: Satagopan, S.]]	+	[[Category: Satagopan, S]]
-	[[Category: Spreitzer, R J.]]	+	[[Category: Spreitzer, R J]]
-	[[Category: Taylor, T C.]]	+	[[Category: Taylor, T C]]
	[[Category: Calvin cycle]]		[[Category: Calvin cycle]]
	[[Category: Carbon dioxide fixation]]		[[Category: Carbon dioxide fixation]]

OCA at 06:34, 29 September 2014

OCA — Mon, 29 Sep 2014 06:34:20 GMT

←Older revision		Revision as of 06:34, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2v68.~~png~~\|~~left~~\|200px]]	+	==CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A, T342I==
		+	<StructureSection load='2v68' size='340' side='right' caption='[[2v68]], [[Resolution\|resolution]] 2.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2v68]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V68 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAP:2-CARBOXYARABINITOL-1,5-DIPHOSPHATE'>CAP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MME:N-METHYL+METHIONINE'>MME</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1uw9\|1uw9]], [[1uzh\|1uzh]], [[1gk8\|1gk8]], [[1uwa\|1uwa]], [[1ir2\|1ir2]], [[1uzd\|1uzd]], [[2v63\|2v63]], [[2v67\|2v67]], [[2v69\|2v69]], [[2v6a\|2v6a]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] </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=2v68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v68 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v68 RCSB], [http://www.ebi.ac.uk/pdbsum/2v68 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/v6/2v68_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 loop between alpha-helix 6 and beta-strand 6 in the alpha/beta-barrel of ribulose-1,5-bisphosphate carboxylase/oxygenase plays a key role in discriminating between CO2 and O2. Genetic screening in Chlamydomonas reinhardtii previously identified a loop-6 V331A substitution that decreases carboxylation and CO2/O2 specificity. Revertant selection identified T342I and G344S substitutions that restore photosynthetic growth by increasing carboxylation and specificity of the V331A enzyme. In numerous X-ray crystal structures, loop 6 is closed or open depending on the activation state of the enzyme and the presence or absence of ligands. The carboxy terminus folds over loop 6 in the closed state. To study the molecular basis for catalysis, directed mutagenesis and chloroplast transformation were used to create T342I and G344S substitutions alone. X-ray crystal structures were then solved for the V331A, V331A/T342I, T342I, and V331A/G344S enzymes, as well as for a D473E enzyme created to assess the role of the carboxy terminus in loop-6 closure. V331A disturbs a hydrophobic pocket, abolishing several van der Waals interactions. These changes are complemented by T342I and G344S, both of which alone cause decreases in CO2/O2 specificity. In the V331A/T342I revertant enzyme, Arg339 main-chain atoms are displaced. In V331A/G344S, alpha-helix 6 is shifted. D473E causes disorder of the carboxy terminus, but loop 6 remains closed. Interactions between a transition-state analogue and several residues are altered in the mutant enzymes. However, active-site Lys334 at the apex of loop 6 has a normal conformation. A variety of subtle interactions must be responsible for catalytic efficiency and CO2/O2 specificity.

-	~~{{STRUCTURE_2v68\| PDB=2v68 \| SCENE= }}~~	+	Structural analysis of altered large-subunit loop-6/carboxy-terminus interactions that influence catalytic efficiency and CO2/O2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase.,Karkehabadi S, Satagopan S, Taylor TC, Spreitzer RJ, Andersson I Biochemistry. 2007 Oct 2;46(39):11080-9. Epub 2007 Sep 8. PMID:17824672<ref>PMID:17824672</ref>

-	~~===CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A~~, ~~T342I===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_17824672}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2v68]] is~~ a ~~16 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA].~~	+

	==See Also==		==See Also==
	*[[RuBisCO\|RuBisCO]]		*[[RuBisCO\|RuBisCO]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:017824672<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Chlamydomonas reinhardtii]]		[[Category: Chlamydomonas reinhardtii]]
	[[Category: Ribulose-bisphosphate carboxylase]]		[[Category: Ribulose-bisphosphate carboxylase]]

OCA at 13:56, 20 October 2012

OCA — Sat, 20 Oct 2012 13:56:11 GMT

←Older revision		Revision as of 13:56, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2v68]] is a 16 chain structure ~~of [[RuBisCO]]~~ with sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA].	+	[[2v68]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA].

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

OCA: Protected "2v68" [edit=sysop:move=sysop]

OCA — Thu, 26 Jul 2012 13:33:50 GMT

Protected "2v68" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:33, 26 July 2012

OCA at 13:33, 26 July 2012

OCA — Thu, 26 Jul 2012 13:33:49 GMT

←Older revision		Revision as of 13:33, 26 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2v68.png\|left\|200px]]		[[Image:2v68.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2v68", 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_2v68\| PDB=2v68 \| SCENE= }}		{{STRUCTURE_2v68\| PDB=2v68 \| SCENE= }}

	===CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A, T342I===		===CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A, T342I===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_17824672}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 17824672 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_17824672}}		{{ABSTRACT_PUBMED_17824672}}

	==About this Structure==		==About this Structure==
-	~~2V68~~ is a 16 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA].	+	[[2v68]] is a 16 chain structure of [[RuBisCO]] with sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V68 OCA].
		+
		+	==See Also==
		+	*[[RuBisCO\|RuBisCO]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~17824672~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:017824672</ref><references group="xtra"/>
	[[Category: Chlamydomonas reinhardtii]]		[[Category: Chlamydomonas reinhardtii]]
	[[Category: Ribulose-bisphosphate carboxylase]]		[[Category: Ribulose-bisphosphate carboxylase]]
Line 31:		Line 22:
	[[Category: Spreitzer, R J.]]		[[Category: Spreitzer, R J.]]
	[[Category: Taylor, T C.]]		[[Category: Taylor, T C.]]
-	[[Category: Acetylation]]
	[[Category: Calvin cycle]]		[[Category: Calvin cycle]]
	[[Category: Carbon dioxide fixation]]		[[Category: Carbon dioxide fixation]]
Line 46:		Line 36:
	[[Category: Photorespiration]]		[[Category: Photorespiration]]
	[[Category: Photosynthesis]]		[[Category: Photosynthesis]]
-	[[Category: Plastid]]
	[[Category: Rubisco]]		[[Category: Rubisco]]
	[[Category: Transit peptide]]		[[Category: Transit peptide]]
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-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 10:00:00 2009''