View source for 2pen


==Crystal structure of RbcX, crystal form I==
<StructureSection load='2pen' size='340' side='right'caption='[[2pen]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2pen]] is a 6 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=2PEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PEN 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]] 2.8&#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=2pen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pen OCA], [https://pdbe.org/2pen PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pen RCSB], [https://www.ebi.ac.uk/pdbsum/2pen PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pen ProSAT]</span></td></tr>
</table>
== Function ==
[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> 
== 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/2pen_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=2pen ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synechococcus sp. PCC 7002]]
[[Category: Bracher A]]
[[Category: Hartl FU]]
[[Category: Hayer-Hartl M]]
[[Category: Saschenbrecker S]]
[[Category: Vasudeva Rao B]]
[[Category: Vasudeva Rao K]]