2gio: Difference between revisions
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== | ==Solution Structure of a portion of the 5'UTR of HspA mRNA of Bradyrhizobium japonicum== | ||
Regulatory RNA elements, like riboswitches, respond to intracellular | <StructureSection load='2gio' size='340' side='right'caption='[[2gio]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2gio]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GIO FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2gio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gio OCA], [https://pdbe.org/2gio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gio RCSB], [https://www.ebi.ac.uk/pdbsum/2gio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gio ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Regulatory RNA elements, like riboswitches, respond to intracellular signals by three-dimensional (3D) conformational changes. RNA thermometers employ a similar strategy to sense temperature changes in the cell and regulate the translational machinery. We present here the first 3D NMR structure of the functional domain of a highly conserved bacterial RNA thermometer containing the ribosome binding site that remains occluded at normal temperatures (30 degrees C). We identified a region adjacent to the Shine-Dalgarno sequence that has a network of weak hydrogen bonds within the RNA helix. With the onset of heat shock at 42 degrees C, destabilisation of the RNA structure initiates at this region and favours the release of the ribosome binding site and of the start codon. Deletion of a highly conserved G residue leads to the formation of a stable regular RNA helix that loses thermosensing ability. Our results indicate that RNA thermometers are able to sense temperature changes without the aid of accessory factors. | |||
Molecular basis for temperature sensing by an RNA thermometer.,Chowdhury S, Maris C, Allain FH, Narberhaus F EMBO J. 2006 Jun 7;25(11):2487-97. Epub 2006 May 18. PMID:16710302<ref>PMID:16710302</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 2gio" style="background-color:#fffaf0;"></div> | ||
[[Category: Allain | == References == | ||
[[Category: Chowdhury | <references/> | ||
[[Category: Maris | __TOC__ | ||
[[Category: Narberhaus | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Allain FH]] | |||
[[Category: Chowdhury S]] | |||
[[Category: Maris C]] | |||
[[Category: Narberhaus F]] |
Latest revision as of 19:36, 13 December 2023
Solution Structure of a portion of the 5'UTR of HspA mRNA of Bradyrhizobium japonicumSolution Structure of a portion of the 5'UTR of HspA mRNA of Bradyrhizobium japonicum
Structural highlights
Publication Abstract from PubMedRegulatory RNA elements, like riboswitches, respond to intracellular signals by three-dimensional (3D) conformational changes. RNA thermometers employ a similar strategy to sense temperature changes in the cell and regulate the translational machinery. We present here the first 3D NMR structure of the functional domain of a highly conserved bacterial RNA thermometer containing the ribosome binding site that remains occluded at normal temperatures (30 degrees C). We identified a region adjacent to the Shine-Dalgarno sequence that has a network of weak hydrogen bonds within the RNA helix. With the onset of heat shock at 42 degrees C, destabilisation of the RNA structure initiates at this region and favours the release of the ribosome binding site and of the start codon. Deletion of a highly conserved G residue leads to the formation of a stable regular RNA helix that loses thermosensing ability. Our results indicate that RNA thermometers are able to sense temperature changes without the aid of accessory factors. Molecular basis for temperature sensing by an RNA thermometer.,Chowdhury S, Maris C, Allain FH, Narberhaus F EMBO J. 2006 Jun 7;25(11):2487-97. Epub 2006 May 18. PMID:16710302[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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