2peq

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{{Seed}}
 
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[[Image:2peq.png|left|200px]]
 
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==Crystal structure of RbcX, crystal form II==
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The line below this paragraph, containing "STRUCTURE_2peq", creates the "Structure Box" on the page.
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<StructureSection load='2peq' size='340' side='right'caption='[[2peq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2peq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_sp._PCC_7002 Synechococcus sp. PCC 7002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PEQ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2peq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2peq OCA], [https://pdbe.org/2peq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2peq RCSB], [https://www.ebi.ac.uk/pdbsum/2peq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2peq ProSAT]</span></td></tr>
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{{STRUCTURE_2peq| PDB=2peq | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RBCX_SYNP2 RBCX_SYNP2] An RbcL-specific chaperone. Required for assembly of the RbcL8 core, acting downstream of the major chaperonin (GroEL-GroES). Acts on newly folded RbcL, has a transient dynamic interaction with RbcL and is eventually displaced by RbcS (PubMed:17574029). 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 (By similarity). Required for optimal reconstitution of RuBisCO into its RbcL8S8 holoenzyme form upon expression of rbcL-rbcS subunits in E.coli, and probably also in situ. A frameshift mutation that replaces half the protein reduces accumulation of both RbcL and RbcS subunits and halves activity of RuBisCO in situ and in E.coli (PubMed:15564522).[UniProtKB:Q44212]<ref>PMID:15564522</ref> <ref>PMID:17574029</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pe/2peq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2peq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal structure of RbcX, crystal form II===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2peq" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17574029 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17574029}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2PEQ is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Synechococcus_sp._pcc_7002 Synechococcus sp. pcc 7002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PEQ OCA].
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[[Category: Synechococcus sp. PCC 7002]]
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[[Category: Bracher A]]
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==Reference==
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[[Category: Hartl FU]]
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<ref group="xtra">PMID:17574029</ref><references group="xtra"/>
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[[Category: Hayer-Hartl M]]
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[[Category: Synechococcus sp. pcc 7002]]
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[[Category: Saschenbrecker S]]
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[[Category: Bracher, A.]]
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[[Category: Vasudeva Rao B]]
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[[Category: Hartl, F U.]]
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[[Category: Vasudeva Rao K]]
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[[Category: Hayer-Hartl, M.]]
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[[Category: Rao, B Vasudeva.]]
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[[Category: Rao, K Vasudeva.]]
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[[Category: Saschenbrecker, S.]]
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[[Category: Chaperone]]
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[[Category: Helix bundle]]
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[[Category: Protein complex assembly]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 00:44:15 2009''
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Current revision

Crystal structure of RbcX, crystal form II

PDB ID 2peq

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