5bs2 - Revision history

OCA at 11:17, 10 January 2024

2024-01-10T11:17:10Z

←Older revision		Revision as of 11:17, 10 January 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5bs2]] is a 3 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=5BS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BS2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[5bs2]] is a 3 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=5BS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BS2 FirstGlance]. <br>
-	</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=5bs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bs2 OCA], [https://pdbe.org/5bs2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bs2 RCSB], [https://www.ebi.ac.uk/pdbsum/5bs2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bs2 ProSAT]</span></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]] 1.97Å</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=5bs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bs2 OCA], [https://pdbe.org/5bs2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bs2 RCSB], [https://www.ebi.ac.uk/pdbsum/5bs2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bs2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 06:06, 7 June 2023

2023-06-07T06:06:08Z

←Older revision		Revision as of 06:06, 7 June 2023
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	<StructureSection load='5bs2' size='340' side='right'caption='[[5bs2]], [[Resolution\|resolution]] 1.97Å' scene=''>		<StructureSection load='5bs2' size='340' side='right'caption='[[5bs2]], [[Resolution\|resolution]] 1.97Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5bs2]] is a 3 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=5BS2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5BS2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5bs2]] is a 3 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=5BS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BS2 FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CGL41, CHLREDRAFT_162607 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE]), rbcL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE])</td></tr>	+	</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=5bs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bs2 OCA], [https://pdbe.org/5bs2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bs2 RCSB], [https://www.ebi.ac.uk/pdbsum/5bs2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bs2 ProSAT]</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=5bs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bs2 OCA], [~~http~~://pdbe.org/5bs2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5bs2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5bs2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5bs2 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/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/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]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Chlre~~]]	+	[[Category: Chlamydomonas reinhardtii]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Ribulose-bisphosphate carboxylase]]~~	+	[[Category: Bracher A]]
-	[[Category: Bracher, A]]	+	[[Category: Hartl FU]]
-	[[Category: Hartl~~, F U~~]]	+	[[Category: Hauser T]]
-	[[Category: Hauser, T]]	+	[[Category: Hayer-Hartl M]]
-	[[Category: Hayer-Hartl, M]]	+	[[Category: Liu C]]
-	[[Category: Liu, C]]	+
-	~~[[Category: Chaperone]]~~	+
-	~~[[Category: Rbcx~~]]	+

OCA at 10:58, 18 March 2020

2020-03-18T10:58:45Z

←Older revision		Revision as of 10:58, 18 March 2020
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		+
	==Crystal structure of RbcX-IIa from Chlamydomonas reinhardtii in complex with RbcL C-terminal tail==		==Crystal structure of RbcX-IIa from Chlamydomonas reinhardtii in complex with RbcL C-terminal tail==
-	<StructureSection load='5bs2' size='340' side='right' caption='[[5bs2]], [[Resolution\|resolution]] 1.97Å' scene=''>	+	<StructureSection load='5bs2' size='340' side='right'caption='[[5bs2]], [[Resolution\|resolution]] 1.97Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5bs2]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BS2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BS2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5bs2]] is a 3 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=5BS2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BS2 FirstGlance]. <br>
-	</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>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CGL41, CHLREDRAFT_162607 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE]), rbcL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE])</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=5bs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bs2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5bs2 RCSB], [http://www.ebi.ac.uk/pdbsum/5bs2 PDBsum]</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=5bs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bs2 OCA], [http://pdbe.org/5bs2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bs2 RCSB], [http://www.ebi.ac.uk/pdbsum/5bs2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bs2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 5bs2" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Chlre]]
		+	[[Category: Large Structures]]
	[[Category: Ribulose-bisphosphate carboxylase]]		[[Category: Ribulose-bisphosphate carboxylase]]
	[[Category: Bracher, A]]		[[Category: Bracher, A]]

OCA at 04:49, 9 September 2015

2015-09-09T04:49:29Z

←Older revision		Revision as of 04:49, 9 September 2015
Line 8:		Line 8:
	== 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/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/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/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]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The most prevalent form of the Rubisco enzyme is a complex of eight catalytic large subunits (RbcL) and eight regulatory small subunits (RbcS). Rubisco biogenesis depends on the assistance by specific molecular chaperones. The assembly chaperone RbcX stabilizes the RbcL subunits after folding by chaperonin and mediates their assembly to the RbcL8 core complex, from which RbcX is displaced by RbcS to form active holoenzyme. Two isoforms of RbcX are found in eukaryotes, RbcX-I, which is more closely related to cyanobacterial RbcX, and the more distant RbcX-II. The green algae Chlamydomonas reinhardtii contains only RbcX-II isoforms, CrRbcX-IIa and CrRbcX-IIb. Here we solved the crystal structure of CrRbcX-IIa and show that it forms an arc-shaped dimer with a central hydrophobic cleft for binding the C-terminal sequence of RbcL. Like other RbcX proteins, CrRbcX-IIa supports the assembly of cyanobacterial Rubisco in vitro, albeit with reduced activity relative to cyanobacterial RbcX-I. Structural analysis of a fusion protein of CrRbcX-IIa and the C-terminal peptide of RbcL suggests that the peptide binding mode of RbcX-II may differ from that of cyanobacterial RbcX. RbcX homologs appear to have adapted to their cognate Rubisco clients as a result of co-evolution.
		+
		+	Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii.,Bracher A, Hauser T, Liu C, Hartl FU, Hayer-Hartl M PLoS One. 2015 Aug 25;10(8):e0135448. doi: 10.1371/journal.pone.0135448., eCollection 2015. PMID:26305355<ref>PMID:26305355</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 20:19, 5 August 2015

2015-08-05T20:19:29Z

←Older revision		Revision as of 20:19, 5 August 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of RbcX-IIa from Chlamydomonas reinhardtii in complex with RbcL C-terminal tail==
-		+	<StructureSection load='5bs2' size='340' side='right' caption='[[5bs2]], [[Resolution\|resolution]] 1.97Å' scene=''>
-	~~The entry~~ 5bs2 is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5bs2]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BS2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BS2 FirstGlance]. <br>
-	~~Authors~~: ~~Bracher~~, A.	+	</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=5bs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bs2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5bs2 RCSB], [http://www.ebi.ac.uk/pdbsum/5bs2 PDBsum]</span></td></tr>
-	~~Description~~:	+	</table>
-	[[Category: ~~Unreleased Structures~~]]	+	== 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/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]
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Ribulose-bisphosphate carboxylase]]
	[[Category: Bracher, A]]		[[Category: Bracher, A]]
		+	[[Category: Hartl, F U]]
		+	[[Category: Hauser, T]]
		+	[[Category: Hayer-Hartl, M]]
		+	[[Category: Liu, C]]
		+	[[Category: Chaperone]]
		+	[[Category: Rbcx]]

OCA at 11:51, 15 July 2015

2015-07-15T11:51:47Z

←Older revision		Revision as of 11:51, 15 July 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5bs2 is ON HOLD	+	The entry 5bs2 is ON HOLD until Paper Publication

	Authors: Bracher, A.		Authors: Bracher, A.

OCA at 13:23, 8 July 2015

2015-07-08T13:23:16Z

←Older revision		Revision as of 13:23, 8 July 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5bs2 is ON HOLD ~~until sometime in the future~~	+	The entry 5bs2 is ON HOLD

	Authors: Bracher, A.		Authors: Bracher, A.

OCA at 13:50, 17 June 2015

2015-06-17T13:50:45Z

←Older revision		Revision as of 13:50, 17 June 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5bs2 is ON HOLD	+	The entry 5bs2 is ON HOLD until sometime in the future

	Authors: Bracher, A.		Authors: Bracher, A.

OCA: Protected "5bs2" [edit=sysop:move=sysop]

2015-06-10T12:58:53Z

Protected "5bs2" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:58, 10 June 2015

OCA: New page: '''Unreleased structure''' The entry 5bs2 is ON HOLD Authors: Bracher, A. Description: Category: Unreleased Structures Category: Bracher, A

2015-06-10T12:58:52Z

New page: '''Unreleased structure''' The entry 5bs2 is ON HOLD Authors: Bracher, A. Description: Category: Unreleased Structures Category: Bracher, A

New page

'''Unreleased structure'''

The entry 5bs2 is ON HOLD

Authors: Bracher, A.

Description:
[[Category: Unreleased Structures]]
[[Category: Bracher, A]]