2ldt
From Proteopedia
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==The 912-888 alternate conformation for helix 27 of E.coli 16S rRNA== | ==The 912-888 alternate conformation for helix 27 of E.coli 16S rRNA== | ||
| - | <StructureSection load='2ldt' size='340' side='right' caption='[[2ldt | + | <StructureSection load='2ldt' size='340' side='right'caption='[[2ldt]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | [[2ldt]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDT OCA]. | + | <table><tr><td colspan='2'>[[2ldt]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LDT FirstGlance]. <br> |
| - | <b> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ldt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ldt OCA], [https://pdbe.org/2ldt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ldt RCSB], [https://www.ebi.ac.uk/pdbsum/2ldt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ldt ProSAT]</span></td></tr> |
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Helix (H)27 of 16S ribosomal (r)RNA from Escherichia coli was dubbed the "switch helix" when mutagenesis suggested that two alternative base pair registers may have distinct functional roles in the bacterial ribosome. Although more recent genetic analyses suggest that H27 conformational switching is not required for translation, previous solution studies demonstrated that the isolated E. coli H27 can dynamically convert between the 885 and 888 conformations. Here, we have solved the nuclear magnetic resonance solution structure of a locked 888 conformation. NOE and residual dipolar coupling restraints reveal an architecture that markedly differs from that of the 885 conformation found in crystal structures of the bacterial ribosome. In place of the loop E motif that characterizes the 885 conformer and that the 888 conformer cannot adopt, we find evidence for an asymmetrical A-rich internal loop stabilized by stacking interactions among the unpaired A's. Comparison of the isolated H27 888 solution structure with the 885 crystal structure within the context of the ribosome suggests a difference in overall length of H27 that presents one plausible reason for the absence of H27 conformational switching within the sterically confining ribosome. (c) 2011 Wiley Periodicals, Inc. Biopolymers 95: 653-668, 2011. | Helix (H)27 of 16S ribosomal (r)RNA from Escherichia coli was dubbed the "switch helix" when mutagenesis suggested that two alternative base pair registers may have distinct functional roles in the bacterial ribosome. Although more recent genetic analyses suggest that H27 conformational switching is not required for translation, previous solution studies demonstrated that the isolated E. coli H27 can dynamically convert between the 885 and 888 conformations. Here, we have solved the nuclear magnetic resonance solution structure of a locked 888 conformation. NOE and residual dipolar coupling restraints reveal an architecture that markedly differs from that of the 885 conformation found in crystal structures of the bacterial ribosome. In place of the loop E motif that characterizes the 885 conformer and that the 888 conformer cannot adopt, we find evidence for an asymmetrical A-rich internal loop stabilized by stacking interactions among the unpaired A's. Comparison of the isolated H27 888 solution structure with the 885 crystal structure within the context of the ribosome suggests a difference in overall length of H27 that presents one plausible reason for the absence of H27 conformational switching within the sterically confining ribosome. (c) 2011 Wiley Periodicals, Inc. Biopolymers 95: 653-668, 2011. | ||
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Solution structure of an alternate conformation of helix27 from Escherichia coli16S rRNA.,Spano MN, Walter NG Biopolymers. 2011 Oct;95(10):653-68. doi: 10.1002/bip.21626. Epub 2011 Mar, 25. PMID:21442607<ref>PMID:21442607</ref> | Solution structure of an alternate conformation of helix27 from Escherichia coli16S rRNA.,Spano MN, Walter NG Biopolymers. 2011 Oct;95(10):653-68. doi: 10.1002/bip.21626. Epub 2011 Mar, 25. PMID:21442607<ref>PMID:21442607</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> | ||
| + | <div class="pdbe-citations 2ldt" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Spano MN]] |
| - | [[Category: | + | [[Category: Walter NG]] |
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| - | + | ||
Current revision
The 912-888 alternate conformation for helix 27 of E.coli 16S rRNA
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