2n88

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'''Unreleased structure'''
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==Chromodomain 3 (CD3) of cpSRP43==
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<StructureSection load='2n88' size='340' side='right' caption='[[2n88]], [[NMR_Ensembles_of_Models | 9 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2n88]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N88 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N88 FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n88 OCA], [http://pdbe.org/2n88 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n88 RCSB], [http://www.ebi.ac.uk/pdbsum/2n88 PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/SR43C_ARATH SR43C_ARATH]] Component of the chloroplast signal recognition particle pathway. Required for post-translational targeting of proteins into the tylakoid membrane but seems to be dispensable for co-translational targeting with a translating ribosome present. May be able to function independently of cpFTSY and FFC/cpSRP54 in targeting LHCPs to the thylakoids. Acts as a highly specific chaperone for LHCPs, preventing aggregation and being able to dissolve aggregates.<ref>PMID:9878634</ref> <ref>PMID:10480939</ref> <ref>PMID:15292240</ref> <ref>PMID:17513500</ref> <ref>PMID:20498370</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Canonical membrane protein biogenesis requires co-translational delivery of ribosome-associated proteins to the Sec translocase and depends on the signal recognition particle (SRP) and its receptor (SR). In contrast, high-throughput delivery of abundant light-harvesting chlorophyll a,b-binding proteins (LHCPs) in chloroplasts to the Alb3 insertase occurs post-translationally via a soluble transit complex including the cpSRP43/cpSRP54 heterodimer (cpSRP). Here we describe the molecular mechanisms of tethering cpSRP to the Alb3 insertase by specific interaction of cpSRP43 chromodomain 3 with a linear motif in the Alb3 C-terminal tail. Combining NMR spectroscopy, X-ray crystallography and biochemical analyses, we dissect the structural basis for selectivity of chromodomains 2 and 3 for their respective ligands cpSRP54 and Alb3, respectively. Negative cooperativity in ligand binding can be explained by dynamics in the chromodomain interface. Our study provides a model for membrane recruitment of the transit complex and may serve as a prototype for a functional gain by the tandem arrangement of chromodomains.
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The entry 2n88 is ON HOLD
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Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction.,Horn A, Hennig J, Ahmed YL, Stier G, Wild K, Sattler M, Sinning I Nat Commun. 2015 Nov 16;6:8875. doi: 10.1038/ncomms9875. PMID:26568381<ref>PMID:26568381</ref>
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Authors: Hennig, J., Sattler, M.
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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>
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Description: Chromodomain 3 (CD3) of cpSRP43
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<div class="pdbe-citations 2n88" style="background-color:#fffaf0;"></div>
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[[Category: Unreleased Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Hennig, J]]
[[Category: Hennig, J]]
[[Category: Sattler, M]]
[[Category: Sattler, M]]
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[[Category: Chromodomain]]
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[[Category: Cpsrp]]
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[[Category: Membrane trafficking]]
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[[Category: Plant signaling]]
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[[Category: Protein binding]]
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[[Category: Srp]]

Revision as of 13:43, 9 December 2015

Chromodomain 3 (CD3) of cpSRP43

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