View source for 8bvj


==Hfq-Crc-estA translation repression complex==
<StructureSection load='8bvj' size='340' side='right'caption='[[8bvj]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8bvj]] is a 23 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BVJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BVJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.5&#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=8bvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bvj OCA], [https://pdbe.org/8bvj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bvj RCSB], [https://www.ebi.ac.uk/pdbsum/8bvj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bvj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HFQ_PSEA7 HFQ_PSEA7] RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The widely occurring bacterial RNA chaperone Hfq is a key factor in the post-transcriptional control of hundreds of genes in Pseudomonas aeruginosa. How this broadly acting protein can contribute to the regulatory requirements of many different genes remains puzzling. Here, we describe cryo-EM structures of higher order assemblies formed by Hfq and its partner protein Crc on control regions of different P. aeruginosa target mRNAs. Our results show that these assemblies have mRNA-specific quaternary architectures resulting from the combination of multivalent protein-protein interfaces and recognition of patterns in the RNA sequence. The structural polymorphism of these ribonucleoprotein assemblies enables selective translational repression of many different target mRNAs. This system elucidates how highly complex regulatory pathways can evolve with a minimal economy of proteinogenic components in combination with RNA sequence and fold.

Translational regulation by Hfq-Crc assemblies emerges from polymorphic ribonucleoprotein folding.,Dendooven T, Sonnleitner E, Blasi U, Luisi BF EMBO J. 2023 Feb 1;42(3):e111129. doi: 10.15252/embj.2022111129. Epub 2022 Dec , 12. PMID:36504222<ref>PMID:36504222</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8bvj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Protein Hfq 3D structures|Protein Hfq 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Dendooven T]]
[[Category: Luisi BF]]