8bvm: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Cryo-EM structure of Hfq-Crc-rbsB translation repression complex== | ==Cryo-EM structure of Hfq-Crc-rbsB translation repression complex== | ||
<StructureSection load='8bvm' size='340' side='right'caption='[[8bvm]], [[Resolution|resolution]] 3. | <StructureSection load='8bvm' size='340' side='right'caption='[[8bvm]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
== Structural highlights == | == 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> | <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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8Å</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> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ | [https://www.uniprot.org/uniprot/Q51380_PSEAI Q51380_PSEAI] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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. | 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. | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 8bvm" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 8bvm" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Protein Hfq 3D structures|Protein Hfq 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 09:49, 24 July 2024
Cryo-EM structure of Hfq-Crc-rbsB translation repression complexCryo-EM structure of Hfq-Crc-rbsB translation repression complex
Structural highlights
FunctionPublication 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. 2023 Feb 1;42(3):e111129. doi: 10.15252/embj.2022111129. Epub 2022 Dec , 12. PMID:36504222[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||