1rsc - Revision history

OCA at 08:26, 1 May 2024

2024-05-01T08:26:36Z

←Older revision		Revision as of 08:26, 1 May 2024
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	<StructureSection load='1rsc' size='340' side='right'caption='[[1rsc]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1rsc' size='340' side='right'caption='[[1rsc]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1rsc]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Anacystis_nidulans Anacystis nidulans~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RSC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1rsc]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_6301 Synechococcus elongatus PCC 6301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RSC FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=XBP:XYLULOSE~~-1,~~5-BISPHOSPHATE'>XBP</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='~~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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XBP:XYLULOSE-1,5-BISPHOSPHATE'>XBP</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=1rsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsc OCA], [https://pdbe.org/1rsc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rsc RCSB], [https://www.ebi.ac.uk/pdbsum/1rsc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rsc 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=1rsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsc OCA], [https://pdbe.org/1rsc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rsc RCSB], [https://www.ebi.ac.uk/pdbsum/1rsc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rsc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/RBL_SYNP6 RBL_SYNP6]] 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/RBS_SYNP6 RBS_SYNP6]] 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_SYNP6 RBL_SYNP6] 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]]
Line 20:		Line 20:
	</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=1rsc 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=1rsc ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	BACKGROUND: Ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) catalyzes the addition of CO2 to ribulose 1,5-bisphosphate in all photosynthetic organisms. During catalysis, the bisphosphate is depleted by reactions other than carboxylation and some of the products are potent inhibitors of rubisco. We have used one of these, xylulose 1,5-bisphosphate as an analogue of the natural substrate and co-crystallized it with the enzyme. RESULTS: We have solved the crystal structure of Synechococcus rubisco with bound xylulose 1,5-bisphosphate to 2.3 A and compared it with the previously solved 2'-carboxylarabinitol 1,5-bisphosphate (2CABP) enzyme quaternary complex. Unlike 2CABP, xylulose 1,5-bisphosphate forms a binary complex with no activating CO2 or essential metal present. Five flexible elements that restrict access to the active site in the 2CABP complex also close off the active site in the xylulose 1,5-bisphosphate complex, stabilized by interactions with the hydrated form of the analogue. CONCLUSIONS: Xylulose 1,5-bisphosphate induces closure of critical loops of the protein without essential cofactors resident at the active site. In the case of rubisco in one species, catalysis is completely inhibited.
-
-	Structure of an effector-induced inactivated state of ribulose 1,5-bisphosphate carboxylase/oxygenase: the binary complex between enzyme and xylulose 1,5-bisphosphate.,Newman J, Gutteridge S Structure. 1994 Jun 15;2(6):495-502. PMID:7922027<ref>PMID:7922027</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1rsc" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[RuBisCO 3D structures\|RuBisCO 3D structures]]		*[[RuBisCO 3D structures\|RuBisCO 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Anacystis nidulans]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Ribulose-bisphosphate carboxylase~~]]	+	[[Category: Synechococcus elongatus PCC 6301]]
-	[[Category: Gutteridge, S]]	+	[[Category: Gutteridge S]]
-	[[Category: Newman, J]]	+	[[Category: Newman J]]

OCA at 07:20, 22 September 2021

2021-09-22T07:20:54Z

←Older revision		Revision as of 07:20, 22 September 2021
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	<StructureSection load='1rsc' size='340' side='right'caption='[[1rsc]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1rsc' size='340' side='right'caption='[[1rsc]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1rsc]] is a 16 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Anacystis_nidulans Anacystis nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1RSC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1rsc]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Anacystis_nidulans Anacystis nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RSC FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XBP:XYLULOSE-1,5-BISPHOSPHATE'>XBP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XBP:XYLULOSE-1,5-BISPHOSPHATE'>XBP</scene></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=1rsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsc OCA], [~~http~~://pdbe.org/1rsc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1rsc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1rsc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1rsc 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=1rsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsc OCA], [https://pdbe.org/1rsc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rsc RCSB], [https://www.ebi.ac.uk/pdbsum/1rsc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rsc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/RBL_SYNP6 RBL_SYNP6]] 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/RBS_SYNP6 RBS_SYNP6]] 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_SYNP6 RBL_SYNP6]] 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/RBS_SYNP6 RBS_SYNP6]] 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 31:		Line 31:

	==See Also==		==See Also==
-	*[[RuBisCO\|RuBisCO]]	+	*[[RuBisCO 3D structures\|RuBisCO 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:26, 11 December 2019

2019-12-11T19:26:44Z

←Older revision		Revision as of 19:26, 11 December 2019
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	==STRUCTURE OF AN EFFECTOR INDUCED INACTIVATED STATE OF RIBULOSE BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE: THE BINARY COMPLEX BETWEEN ENZYME AND XYLULOSE BISPHOSPHATE==		==STRUCTURE OF AN EFFECTOR INDUCED INACTIVATED STATE OF RIBULOSE BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE: THE BINARY COMPLEX BETWEEN ENZYME AND XYLULOSE BISPHOSPHATE==
-	<StructureSection load='1rsc' size='340' side='right' caption='[[1rsc]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='1rsc' size='340' side='right'caption='[[1rsc]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1rsc]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Anacystis_nidulans Anacystis nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RSC FirstGlance]. <br>		<table><tr><td colspan='2'>[[1rsc]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Anacystis_nidulans Anacystis nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RSC FirstGlance]. <br>
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Anacystis nidulans]]		[[Category: Anacystis nidulans]]
		+	[[Category: Large Structures]]
	[[Category: Ribulose-bisphosphate carboxylase]]		[[Category: Ribulose-bisphosphate carboxylase]]
	[[Category: Gutteridge, S]]		[[Category: Gutteridge, S]]
	[[Category: Newman, J]]		[[Category: Newman, J]]

OCA at 06:58, 8 March 2018

2018-03-08T06:58:11Z

←Older revision		Revision as of 06:58, 8 March 2018
Line 1:		Line 1:
		+
	==STRUCTURE OF AN EFFECTOR INDUCED INACTIVATED STATE OF RIBULOSE BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE: THE BINARY COMPLEX BETWEEN ENZYME AND XYLULOSE BISPHOSPHATE==		==STRUCTURE OF AN EFFECTOR INDUCED INACTIVATED STATE OF RIBULOSE BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE: THE BINARY COMPLEX BETWEEN ENZYME AND XYLULOSE BISPHOSPHATE==
	<StructureSection load='1rsc' size='340' side='right' caption='[[1rsc]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1rsc' size='340' side='right' caption='[[1rsc]], [[Resolution\|resolution]] 2.30Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XBP:XYLULOSE-1,5-BISPHOSPHATE'>XBP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XBP:XYLULOSE-1,5-BISPHOSPHATE'>XBP</scene></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=1rsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsc OCA], [http://pdbe.org/1rsc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rsc RCSB], [http://www.ebi.ac.uk/pdbsum/1rsc 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=1rsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsc OCA], [http://pdbe.org/1rsc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rsc RCSB], [http://www.ebi.ac.uk/pdbsum/1rsc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rsc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rs/1rsc_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rs/1rsc_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 09:44, 9 February 2016

2016-02-09T09:44:12Z

←Older revision		Revision as of 09:44, 9 February 2016
Line 17:		Line 17:
	<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=1rsc ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 20:59, 10 September 2015

2015-09-10T20:59:53Z

←Older revision		Revision as of 20:59, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1rsc' size='340' side='right' caption='[[1rsc]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1rsc' size='340' side='right' caption='[[1rsc]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1rsc]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Synechococcus_elongatus Synechococcus elongatus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RSC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1rsc]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Anacystis_nidulans Anacystis nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RSC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XBP:XYLULOSE-1,5-BISPHOSPHATE'>XBP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XBP:XYLULOSE-1,5-BISPHOSPHATE'>XBP</scene></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=1rsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rsc RCSB], [http://www.ebi.ac.uk/pdbsum/1rsc 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=1rsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsc OCA], [http://pdbe.org/1rsc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rsc RCSB], [http://www.ebi.ac.uk/pdbsum/1rsc PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1rsc" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Anacystis nidulans]]
	[[Category: Ribulose-bisphosphate carboxylase]]		[[Category: Ribulose-bisphosphate carboxylase]]
-	[[Category: Synechococcus elongatus]]
	[[Category: Gutteridge, S]]		[[Category: Gutteridge, S]]
	[[Category: Newman, J]]		[[Category: Newman, J]]

OCA at 06:02, 25 December 2014

2014-12-25T06:02:59Z

←Older revision		Revision as of 06:02, 25 December 2014
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1rsc]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RSC FirstGlance]. <br>		<table><tr><td colspan='2'>[[1rsc]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RSC FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XBP:XYLULOSE-1,5-BISPHOSPHATE'>XBP</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XBP:XYLULOSE-1,5-BISPHOSPHATE'>XBP</scene></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=1rsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rsc RCSB], [http://www.ebi.ac.uk/pdbsum/1rsc 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=1rsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rsc RCSB], [http://www.ebi.ac.uk/pdbsum/1rsc PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RBL_SYNP6 RBL_SYNP6]] 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/RBS_SYNP6 RBS_SYNP6]] 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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	[[Category: Ribulose-bisphosphate carboxylase]]		[[Category: Ribulose-bisphosphate carboxylase]]
	[[Category: Synechococcus elongatus]]		[[Category: Synechococcus elongatus]]
-	[[Category: Gutteridge, S.]]	+	[[Category: Gutteridge, S]]
-	[[Category: Newman, J.]]	+	[[Category: Newman, J]]

OCA at 23:25, 28 September 2014

2014-09-28T23:25:06Z

←Older revision		Revision as of 23:25, 28 September 2014
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-	[[~~Image~~:1rsc.~~png\|left~~\|200px]]	+	==STRUCTURE OF AN EFFECTOR INDUCED INACTIVATED STATE OF RIBULOSE BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE: THE BINARY COMPLEX BETWEEN ENZYME AND XYLULOSE BISPHOSPHATE==
		+	<StructureSection load='1rsc' size='340' side='right' caption='[[1rsc]], [[Resolution\|resolution]] 2.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1rsc]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RSC FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XBP:XYLULOSE-1,5-BISPHOSPHATE'>XBP</scene><br>
		+	<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=1rsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rsc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rsc RCSB], [http://www.ebi.ac.uk/pdbsum/1rsc 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/rs/1rsc_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 ==
		+	BACKGROUND: Ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) catalyzes the addition of CO2 to ribulose 1,5-bisphosphate in all photosynthetic organisms. During catalysis, the bisphosphate is depleted by reactions other than carboxylation and some of the products are potent inhibitors of rubisco. We have used one of these, xylulose 1,5-bisphosphate as an analogue of the natural substrate and co-crystallized it with the enzyme. RESULTS: We have solved the crystal structure of Synechococcus rubisco with bound xylulose 1,5-bisphosphate to 2.3 A and compared it with the previously solved 2'-carboxylarabinitol 1,5-bisphosphate (2CABP) enzyme quaternary complex. Unlike 2CABP, xylulose 1,5-bisphosphate forms a binary complex with no activating CO2 or essential metal present. Five flexible elements that restrict access to the active site in the 2CABP complex also close off the active site in the xylulose 1,5-bisphosphate complex, stabilized by interactions with the hydrated form of the analogue. CONCLUSIONS: Xylulose 1,5-bisphosphate induces closure of critical loops of the protein without essential cofactors resident at the active site. In the case of rubisco in one species, catalysis is completely inhibited.

-	~~{{STRUCTURE_1rsc\| PDB=1rsc \| SCENE= }}~~	+	Structure of an effector-induced inactivated state of ribulose 1,5-bisphosphate carboxylase/oxygenase: the binary complex between enzyme and xylulose 1,5-bisphosphate.,Newman J, Gutteridge S Structure. 1994 Jun 15;2(6):495-502. PMID:7922027<ref>PMID:7922027</ref>

-	~~===STRUCTURE OF AN EFFECTOR INDUCED INACTIVATED STATE OF RIBULOSE BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE: THE BINARY COMPLEX BETWEEN ENZYME AND XYLULOSE BISPHOSPHATE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_7922027}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1rsc]] is~~ a ~~16 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Synechococcus_elongatus Synechococcus elongatus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1RSC OCA].~~	+

	==See Also==		==See Also==
	*[[RuBisCO\|RuBisCO]]		*[[RuBisCO\|RuBisCO]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:007922027<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Ribulose-bisphosphate carboxylase]]		[[Category: Ribulose-bisphosphate carboxylase]]
	[[Category: Synechococcus elongatus]]		[[Category: Synechococcus elongatus]]
	[[Category: Gutteridge, S.]]		[[Category: Gutteridge, S.]]
	[[Category: Newman, J.]]		[[Category: Newman, J.]]

OCA at 13:27, 20 October 2012

2012-10-20T13:27:29Z

←Older revision		Revision as of 13:27, 20 October 2012
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	==About this Structure==		==About this Structure==
-	[[1rsc]] is a 16 chain structure ~~of [[RuBisCO]]~~ with sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSC OCA].	+	[[1rsc]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSC OCA].

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

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

2012-07-26T12:02:18Z

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

←Older revision

Revision as of 12:02, 26 July 2012