2wvw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:37, 12 January 2022) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2wvw.png|left|200px]]
 
-
<!--
+
==Cryo-EM structure of the RbcL-RbcX complex==
-
The line below this paragraph, containing "STRUCTURE_2wvw", creates the "Structure Box" on the page.
+
<SX load='2wvw' size='340' side='right' viewer='molstar' caption='[[2wvw]], [[Resolution|resolution]] 9.00&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<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>
-
or leave the SCENE parameter empty for the default display.
+
</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'>[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>
-
{{STRUCTURE_2wvw| PDB=2wvw | SCENE= }}
+
<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 ==
 +
[[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]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wv/2wvw_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/main_output.php?pdb_ID=2wvw ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
===Cryo-EM structure of the RbcL-RbcX complex===
+
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<ref>PMID:20075914</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_20075914}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 2wvw" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 20075914 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_20075914}}
+
-
 
+
-
==About this Structure==
+
-
[[2wvw]] is a 24 chain structure of [[RuBisCO]] with sequence from [http://en.wikipedia.org/wiki/Anabaena_sp._ca Anabaena sp. ca] and [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WVW OCA].
+
==See Also==
==See Also==
-
*[[RuBisCO|RuBisCO]]
+
*[[RuBisCO 3D structures|RuBisCO 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:020075914</ref><references group="xtra"/>
+
__TOC__
-
[[Category: Anabaena sp. ca]]
+
</SX>
 +
[[Category: Anacystis nidulans]]
 +
[[Category: Anasc]]
 +
[[Category: Large Structures]]
[[Category: Ribulose-bisphosphate carboxylase]]
[[Category: Ribulose-bisphosphate carboxylase]]
-
[[Category: Synechococcus elongatus]]
+
[[Category: Beckmann, R]]
-
[[Category: Beckmann, R.]]
+
[[Category: Berninghausen, O]]
-
[[Category: Berninghausen, O.]]
+
[[Category: Bracher, A]]
-
[[Category: Bracher, A.]]
+
[[Category: Hartl, F U]]
-
[[Category: Hartl, F U.]]
+
[[Category: Hayer-Hartl, M]]
-
[[Category: Hayer-Hartl, M.]]
+
[[Category: Liu, C]]
-
[[Category: Liu, C.]]
+
[[Category: Mielke, T]]
-
[[Category: Mielke, T.]]
+
[[Category: Rao, B V]]
-
[[Category: Rao, B V.]]
+
[[Category: Rao, K V]]
-
[[Category: Rao, K V.]]
+
[[Category: Saschenbrecker, S]]
-
[[Category: Saschenbrecker, S.]]
+
[[Category: Starling-Windhof, A]]
-
[[Category: Starling-Windhof, A.]]
+
[[Category: Young, A L]]
-
[[Category: Young, A L.]]
+
[[Category: Calvin cycle]]
[[Category: Calvin cycle]]
[[Category: Carbon dioxide fixation]]
[[Category: Carbon dioxide fixation]]

Current revision

Cryo-EM structure of the RbcL-RbcX complex

2wvw, resolution 9.00Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools