2gio: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2gio.gif|left|200px]]<br /><applet load="2gio" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2gio" />
'''Solution Structure of a portion of the 5'UTR of HspA mRNA of Bradyrhizobium japonicum'''<br />


==Overview==
==Solution Structure of a portion of the 5'UTR of HspA mRNA of Bradyrhizobium japonicum==
<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.
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.


==About this Structure==
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>
2GIO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GIO OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16710302 16710302]
</div>
[[Category: Protein complex]]
<div class="pdbe-citations 2gio" style="background-color:#fffaf0;"></div>
[[Category: Allain, F H.]]
== References ==
[[Category: Chowdhury, S.]]
<references/>
[[Category: Maris, C.]]
__TOC__
[[Category: Narberhaus, F.]]
</StructureSection>
[[Category: g-g non cannonical pair]]
[[Category: Large Structures]]
 
[[Category: Allain FH]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:32:01 2008''
[[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

2gio is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Chowdhury S, Maris C, Allain FH, Narberhaus F. Molecular basis for temperature sensing by an RNA thermometer. EMBO J. 2006 Jun 7;25(11):2487-97. Epub 2006 May 18. PMID:16710302 doi:http://dx.doi.org/7601128
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA