4ht9: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ht9]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HT9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ht9]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HT9 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=4ht9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ht9 OCA], [https://pdbe.org/4ht9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ht9 RCSB], [https://www.ebi.ac.uk/pdbsum/4ht9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ht9 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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=4ht9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ht9 OCA], [https://pdbe.org/4ht9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ht9 RCSB], [https://www.ebi.ac.uk/pdbsum/4ht9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ht9 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[Protein Hfq|Protein Hfq]] | *[[Protein Hfq|Protein Hfq]] | ||
*[[Protein Hfq 3D structures|Protein Hfq 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 18:10, 20 September 2023
Crystal structure of E coli Hfq bound to two RNAsCrystal structure of E coli Hfq bound to two RNAs
Structural highlights
Publication Abstract from PubMedThe rpoS mRNA, which encodes the master regulator sigma(S) of general stress response, requires Hfq-facilitated base pairing with DsrA small RNA for efficient translation at low temperatures. It has recently been proposed that one mechanism underlying Hfq action is to bridge a transient ternary complex by simultaneously binding to rpoS and DsrA. However, no structural evidence of Hfq simultaneously bound to different RNAs has been reported. We detected simultaneous binding of Hfq to rpoS and DsrA fragments. Crystal structures of AU6A*Hfq*A7 and Hfq*A7 complexes were resolved using 1.8- and 1.9-A resolution, respectively. Ternary complex has been further verified in solution by NMR. In vivo, activation of rpoS translation requires intact Hfq, which is capable of bridging rpoS and DsrA simultaneously into ternary complex. This ternary complex possibly corresponds to a meta-stable transition state in Hfq-facilitated small RNA-mRNA annealing process. Hfq-bridged ternary complex is important for translation activation of rpoS by DsrA.,Wang W, Wang L, Wu J, Gong Q, Shi Y Nucleic Acids Res. 2013 Jun 1;41(11):5938-48. doi: 10.1093/nar/gkt276. Epub 2013 , Apr 19. PMID:23605038[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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