View source for 4zoz


==Crystal structure of the Chaetomium thermophilum Sqt1 bound to the N-terminus of the ribosomal protein L10==
<StructureSection load='4zoz' size='340' side='right'caption='[[4zoz]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4zoz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZOZ 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]] 1.7&#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=4zoz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zoz OCA], [https://pdbe.org/4zoz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zoz RCSB], [https://www.ebi.ac.uk/pdbsum/4zoz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zoz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G0S0R0_CHATD G0S0R0_CHATD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Exponentially growing yeast cells produce every minute &gt;160,000 ribosomal proteins. Owing to their difficult physicochemical properties, the synthesis of assembly-competent ribosomal proteins represents a major challenge. Recent evidence highlights that dedicated chaperone proteins recognize the N-terminal regions of ribosomal proteins and promote their soluble expression and delivery to the assembly site. Here we explore the intuitive possibility that ribosomal proteins are captured by dedicated chaperones in a co-translational manner. Affinity purification of four chaperones (Rrb1, Syo1, Sqt1 and Yar1) selectively enriched the mRNAs encoding their specific ribosomal protein clients (Rpl3, Rpl5, Rpl10 and Rps3). X-ray crystallography reveals how the N-terminal, rRNA-binding residues of Rpl10 are shielded by Sqt1's WD-repeat beta-propeller, providing mechanistic insight into the incorporation of Rpl10 into pre-60S subunits. Co-translational capturing of nascent ribosomal proteins by dedicated chaperones constitutes an elegant mechanism to prevent unspecific interactions and aggregation of ribosomal proteins on their road to incorporation.

Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones.,Pausch P, Singh U, Ahmed YL, Pillet B, Murat G, Altegoer F, Stier G, Thoms M, Hurt E, Sinning I, Bange G, Kressler D Nat Commun. 2015 Jun 26;6:7494. doi: 10.1038/ncomms8494. PMID:26112308<ref>PMID:26112308</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4zoz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Chaetomium thermophilum]]
[[Category: Large Structures]]
[[Category: Altegoer F]]
[[Category: Bange G]]
[[Category: Pausch P]]