6o1k: Difference between revisions

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<SX load='6o1k' size='340' side='right' viewer='molstar' caption='[[6o1k]], [[Resolution|resolution]] 3.13&Aring;' scene=''>
<SX load='6o1k' size='340' side='right' viewer='molstar' caption='[[6o1k]], [[Resolution|resolution]] 3.13&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6o1k]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O1K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O1K FirstGlance]. <br>
<table><tr><td colspan='2'>[[6o1k]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] and [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O1K FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exodeoxyribonuclease_III Exodeoxyribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.2 3.1.11.2] </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]] 3.13&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6o1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o1k OCA], [http://pdbe.org/6o1k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o1k RCSB], [http://www.ebi.ac.uk/pdbsum/6o1k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o1k ProSAT]</span></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=6o1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o1k OCA], [https://pdbe.org/6o1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o1k RCSB], [https://www.ebi.ac.uk/pdbsum/6o1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o1k ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HFQ_PSEAE HFQ_PSEAE]] 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 (By similarity).
[https://www.uniprot.org/uniprot/Q51380_PSEAI Q51380_PSEAI]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In diverse bacterial species, the global regulator Hfq contributes to post-transcriptional networks that control expression of numerous genes. Hfq of the opportunistic pathogen Pseudomonas aeruginosa inhibits translation of target transcripts by forming a regulatory complex with the catabolite repression protein Crc. This repressive complex acts part of an intricate mechanism of preferred nutrient utilisation. We describe high-resolution cryo-EM structures of the assembly of Hfq and Crc bound to the translation initiation site of a target mRNA. The core of the assembly is formed through interactions of two cognate RNAs, two Hfq hexamers and a Crc pair. Additional Crc protomers are recruited to the core to generate higher-order assemblies with demonstrated regulatory activity in vivo. This study reveals how Hfq cooperates with a partner protein to regulate translation, and provides a structural basis for an RNA code that guides global regulators to interact cooperatively and regulate different RNA targets.


Architectural principles for Hfq/Crc-mediated regulation of gene expression.,Pei XY, Dendooven T, Sonnleitner E, Chen S, Blasi U, Luisi BF Elife. 2019 Feb 13;8. pii: 43158. doi: 10.7554/eLife.43158. PMID:30758287<ref>PMID:30758287</ref>
==See Also==
 
*[[Protein Hfq 3D structures|Protein Hfq 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6o1k" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Exodeoxyribonuclease III]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Blasi, U]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Chen, S]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Dendooven, T]]
[[Category: Blasi U]]
[[Category: Luisi, B F]]
[[Category: Chen S]]
[[Category: Pei, X Y]]
[[Category: Dendooven T]]
[[Category: Sonnleitner, E]]
[[Category: Luisi BF]]
[[Category: Amie]]
[[Category: Pei XY]]
[[Category: Carbon catabolite repression]]
[[Category: Sonnleitner E]]
[[Category: Crc]]
[[Category: Hfq]]
[[Category: Rna binding protein]]
[[Category: Rna binding protein-rna-hydrolase complex]]
[[Category: Rna-mediated gene regulation]]
[[Category: Rna-protein interaction]]

Latest revision as of 12:22, 20 March 2024

Architectural principles for Hfq/Crc-mediated regulation of gene expression. Hfq-Crc-amiE 2:2:2 complex (core complex)Architectural principles for Hfq/Crc-mediated regulation of gene expression. Hfq-Crc-amiE 2:2:2 complex (core complex)

6o1k, resolution 3.13Å

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