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2wvw

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Cryo-EM structure of the RbcL-RbcX complex

2wvw, resolution 9.00Å

Structural highlights

2wvw is a 24 chain structure with sequence from Anasc and Anacystis nidulans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1rsc, 1rbl
Activity:	Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Form I Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase), a complex of eight large (RbcL) and eight small (RbcS) subunits, catalyses the fixation of atmospheric CO(2) in photosynthesis. The limited catalytic efficiency of Rubisco has sparked extensive efforts to re-engineer the enzyme with the goal of enhancing agricultural productivity. To facilitate such efforts we analysed the formation of cyanobacterial form I Rubisco by in vitro reconstitution and cryo-electron microscopy. We show that RbcL subunit folding by the GroEL/GroES chaperonin is tightly coupled with assembly mediated by the chaperone RbcX(2). RbcL monomers remain partially unstable and retain high affinity for GroEL until captured by RbcX(2). As revealed by the structure of a RbcL(8)-(RbcX(2))(8) assembly intermediate, RbcX(2) acts as a molecular staple in stabilizing the RbcL subunits as dimers and facilitates RbcL(8) core assembly. Finally, addition of RbcS results in RbcX(2) release and holoenzyme formation. Specific assembly chaperones may be required more generally in the formation of complex oligomeric structures when folding is closely coupled to assembly.

Coupled chaperone action in folding and assembly of hexadecameric Rubisco.,Liu C, Young AL, Starling-Windhof A, Bracher A, Saschenbrecker S, Rao BV, Rao KV, Berninghausen O, Mielke T, Hartl FU, Beckmann R, Hayer-Hartl M Nature. 2010 Jan 14;463(7278):197-202. PMID:20075914^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Liu C, Young AL, Starling-Windhof A, Bracher A, Saschenbrecker S, Rao BV, Rao KV, Berninghausen O, Mielke T, Hartl FU, Beckmann R, Hayer-Hartl M. Coupled chaperone action in folding and assembly of hexadecameric Rubisco. Nature. 2010 Jan 14;463(7278):197-202. PMID:20075914 doi:10.1038/nature08651

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wvw"

@@ Line 1: / Line 1: @@
 ==Cryo-EM structure of the RbcL-RbcX complex==
-<StructureSection load='2wvw' size='340' side='right'caption='[[2wvw]], [[Resolution|resolution]] 9.00&Aring;' scene=''>
+<SX load='2wvw' size='340' side='right' viewer='molstar' caption='[[2wvw]], [[Resolution|resolution]] 9.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wvw]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Anasc Anasc] and [http://en.wikipedia.org/wiki/Anacystis_nidulans Anacystis nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WVW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WVW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2wvw]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Anasc Anasc] and [https://en.wikipedia.org/wiki/Anacystis_nidulans Anacystis nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WVW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WVW FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rsc|1rsc]], [[1rbl|1rbl]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rsc|1rsc]], [[1rbl|1rbl]]</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=2wvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wvw OCA], [http://pdbe.org/2wvw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wvw RCSB], [http://www.ebi.ac.uk/pdbsum/2wvw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wvw 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=2wvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wvw OCA], [https://pdbe.org/2wvw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wvw RCSB], [https://www.ebi.ac.uk/pdbsum/2wvw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wvw ProSAT]</span></td></tr>
 </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]
+[[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[RuBisCO|RuBisCO]]
+*[[RuBisCO 3D structures|RuBisCO 3D structures]]
 == References ==
 <references/>
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Anacystis nidulans]]
 [[Category: Anasc]]

2wvw

From Proteopedia

Current revision

Cryo-EM structure of the RbcL-RbcX complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

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