2pek: Difference between revisions

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 ==Crystal structure of RbcX point mutant Q29A==
-<StructureSection load='2pek' size='340' side='right' caption='[[2pek]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+<StructureSection load='2pek' size='340' side='right'caption='[[2pek]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2pek]] is a 6 chain structure with sequence 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=2PEK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PEK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2pek]] 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=2PEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PEK FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pei|2pei]], [[2pej|2pej]], [[2pem|2pem]], [[2pen|2pen]], [[2peo|2peo]], [[2peq|2peq]]</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]] 3.1&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RbcX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32049 Synechococcus sp. PCC 7002])</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=2pek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pek OCA], [https://pdbe.org/2pek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pek RCSB], [https://www.ebi.ac.uk/pdbsum/2pek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pek ProSAT]</span></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pek OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pek RCSB], [http://www.ebi.ac.uk/pdbsum/2pek PDBsum]</span></td></tr>
+</table>
-<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/2pek_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pe/2pek_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/chain_selection.php?pdb_ID=2ata 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=2pek ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2pek" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Synechococcus sp. pcc 7002]]
+[[Category: Large Structures]]
-[[Category: Bracher, A.]]
+[[Category: Synechococcus sp. PCC 7002]]
-[[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]]