8bvm: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
The | ==Cryo-EM structure of Hfq-Crc-rbsB translation repression complex== | ||
<StructureSection load='8bvm' size='340' side='right'caption='[[8bvm]], [[Resolution|resolution]] 3.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8bvm]] is a 16 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=8BVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BVM FirstGlance]. <br> | |||
</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=8bvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bvm OCA], [https://pdbe.org/8bvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bvm RCSB], [https://www.ebi.ac.uk/pdbsum/8bvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bvm 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. 2022 Dec 12:e111129. doi: 10.15252/embj.2022111129. PMID:36504222<ref>PMID:36504222</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Dendooven | <div class="pdbe-citations 8bvm" style="background-color:#fffaf0;"></div> | ||
[[Category: Luisi | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas aeruginosa]] | |||
[[Category: Dendooven T]] | |||
[[Category: Luisi BF]] | |||
Revision as of 09:34, 25 January 2023
Cryo-EM structure of Hfq-Crc-rbsB translation repression complexCryo-EM structure of Hfq-Crc-rbsB translation repression complex
Structural highlights
FunctionHFQ_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. Publication Abstract from PubMedThe 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. 2022 Dec 12:e111129. doi: 10.15252/embj.2022111129. PMID:36504222[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||