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<StructureSection load='2py8' size='340' side='right'caption='[[2py8]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
<StructureSection load='2py8' size='340' side='right'caption='[[2py8]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2py8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PY8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2py8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PY8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</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]] 2.45&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rbcX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1148 Aphanocapsa sp. (strain N-1)])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</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=2py8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py8 OCA], [https://pdbe.org/2py8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2py8 RCSB], [https://www.ebi.ac.uk/pdbsum/2py8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2py8 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=2py8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py8 OCA], [https://pdbe.org/2py8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2py8 RCSB], [https://www.ebi.ac.uk/pdbsum/2py8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2py8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RBCX_SYNY3 RBCX_SYNY3] 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.[HAMAP-Rule:MF_00855]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2py8 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=2py8 ConSurf].
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== Publication Abstract from PubMed ==
In some cyanobacteria, the genes for the large and small subunits of the enzyme RuBisCO are separated on the bacterial chromosome by the insertion of a gene coding for a protein designated RbcX, which acts as a chaperone for RuBisCO. A recent structural study [Saschenbrecker et al. (2007), Cell, 129, 1189-1200] has shed light on the mechanism by which RbcX assists RuBisCO assembly. Here, the crystal structure of RbcX from another cyanobacterium, Synechocystis sp. PCC6803, is reported, revealing an unusually long protruding C-terminal helix, as well as a bound polyethylene glycol molecule in the protein substrate-binding site.
Structure of the RuBisCO chaperone RbcX from Synechocystis sp. PCC6803.,Tanaka S, Sawaya MR, Kerfeld CA, Yeates TO Acta Crystallogr D Biol Crystallogr. 2007 Oct;63(Pt 10):1109-12. Epub 2007, Sep 19. PMID:17881829<ref>PMID:17881829</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2py8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kerfeld, C A]]
[[Category: Synechocystis sp. PCC 6803]]
[[Category: Sawaya, M R]]
[[Category: Kerfeld CA]]
[[Category: Tanaka, S]]
[[Category: Sawaya MR]]
[[Category: Yeates, T O]]
[[Category: Tanaka S]]
[[Category: All helical fold]]
[[Category: Yeates TO]]
[[Category: Chaperone]]

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