5e4x: Difference between revisions
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<StructureSection load='5e4x' size='340' side='right'caption='[[5e4x]], [[Resolution|resolution]] 2.75Å' scene=''> | <StructureSection load='5e4x' size='340' side='right'caption='[[5e4x]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5e4x]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5e4x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E4X FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5e4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e4x OCA], [https://pdbe.org/5e4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e4x RCSB], [https://www.ebi.ac.uk/pdbsum/5e4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e4x ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Arabidopsis thaliana]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ahmed | [[Category: Ahmed YL]] | ||
[[Category: Horn | [[Category: Horn A]] | ||
[[Category: Sinning | [[Category: Sinning I]] | ||
[[Category: Wild | [[Category: Wild K]] | ||
Revision as of 09:12, 5 July 2023
Crystal structure of cpSRP43 chromodomain 3Crystal structure of cpSRP43 chromodomain 3
Structural highlights
FunctionSR43C_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.[1] [2] [3] [4] [5] Publication Abstract from PubMedCanonical 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. 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[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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