2pek: Difference between revisions

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<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 ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2pek]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Agmenellum_quadruplicatum Agmenellum quadruplicatum]. 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>
<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 id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pei|2pei]], [[2pej|2pej]], [[2pem|2pem]], [[2pen|2pen]], [[2peo|2peo]], [[2peq|2peq]]</div></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 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=32049 Agmenellum quadruplicatum])</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 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>
</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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
</StructureSection>
</StructureSection>
[[Category: Agmenellum quadruplicatum]]
[[Category: Large Structures]]
[[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]]

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