2peo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2peo" [edit=sysop:move=sysop])
Current revision (11:00, 30 August 2023) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2peo.png|left|200px]]
 
-
{{STRUCTURE_2peo| PDB=2peo | SCENE= }}
+
==Crystal structure of RbcX from Anabaena CA==
 +
<StructureSection load='2peo' size='340' side='right'caption='[[2peo]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2peo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anabaena_sp._CA_=_ATCC_33047 Anabaena sp. CA = ATCC 33047]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PEO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PEO FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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=2peo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2peo OCA], [https://pdbe.org/2peo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2peo RCSB], [https://www.ebi.ac.uk/pdbsum/2peo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2peo ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/RBCX_ANASC RBCX_ANASC] An RbcL-specific chaperone. The central cleft of the RbcX homodimer (RbcX2) binds the C-terminus of an RbcL monomer, stabilizing the C-terminus and probably preventing its reassociation with chaperonin GroEL-ES. At the same time the peripheral region of RbcX2 binds a second RbcL monomer, bridging the RbcL homodimers in the correct orientation. The RbcX2(2)-bound RbcL dimers then assemble into the RbcL8 core (RbcL8-(RbcX2)8). RbcS binding triggers the release of RbcX2 (PubMed:20075914, PubMed:21765418).[HAMAP-Rule:MF_00855]<ref>PMID:20075914</ref> <ref>PMID:21765418</ref> Required for optimal reconstitution of RuBisCO upon expression of rbcL-rbcS subunits in E.coli (PubMed:9171433).<ref>PMID:9171433</ref>
 +
== 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/pe/2peo_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=2peo ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
After folding, many proteins must assemble into oligomeric complexes to become biologically active. Here we describe the role of RbcX as an assembly chaperone of ribulose-bisphosphate carboxylase/oxygenase (Rubisco), the enzyme responsible for the fixation of atmospheric carbon dioxide. In cyanobacteria and plants, Rubisco is an approximately 520 kDa complex composed of eight large subunits (RbcL) and eight small subunits (RbcS). We found that cyanobacterial RbcX functions downstream of chaperonin-mediated RbcL folding in promoting the formation of RbcL(8) core complexes. Structural analysis revealed that the 15 kDa RbcX forms a homodimer with two cooperating RbcL-binding regions. A central cleft specifically binds the exposed C-terminal peptide of RbcL subunits, enabling a peripheral surface of RbcX to mediate RbcL(8) assembly. Due to the dynamic nature of these interactions, RbcX is readily displaced from RbcL(8) complexes by RbcS, producing the active enzyme. The strategies employed by RbcX in achieving substrate specificity and efficient product release may be generally relevant in assisted assembly reactions.
-
===Crystal structure of RbcX from Anabaena CA===
+
Structure and function of RbcX, an assembly chaperone for hexadecameric Rubisco.,Saschenbrecker S, Bracher A, Rao KV, Rao BV, Hartl FU, Hayer-Hartl M Cell. 2007 Jun 15;129(6):1189-200. PMID:17574029<ref>PMID:17574029</ref>
-
{{ABSTRACT_PUBMED_17574029}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 2peo" style="background-color:#fffaf0;"></div>
-
[[2peo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_sp._ca Anabaena sp. ca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PEO OCA].
+
== References ==
-
 
+
<references/>
-
==Reference==
+
__TOC__
-
<ref group="xtra">PMID:017574029</ref><references group="xtra"/>
+
</StructureSection>
-
[[Category: Anabaena sp. ca]]
+
[[Category: Anabaena sp. CA = ATCC 33047]]
-
[[Category: Bracher, A.]]
+
[[Category: Large Structures]]
-
[[Category: Hartl, F U.]]
+
[[Category: Bracher A]]
-
[[Category: Hayer-Hartl, M.]]
+
[[Category: Hartl FU]]
-
[[Category: Rao, B Vasudeva.]]
+
[[Category: Hayer-Hartl M]]
-
[[Category: Rao, K Vasudeva.]]
+
[[Category: Saschenbrecker S]]
-
[[Category: Saschenbrecker, S.]]
+
[[Category: Vasudeva Rao B]]
-
[[Category: Chaperone]]
+
[[Category: Vasudeva Rao K]]
-
[[Category: Helix bundle]]
+
-
[[Category: Protein complex assembly]]
+

Current revision

Crystal structure of RbcX from Anabaena CA

PDB ID 2peo

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2peo"
Personal tools