4b5r: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[ | ==SAM-I riboswitch bearing the H. marismortui K-t-7== | ||
<StructureSection load='4b5r' size='340' side='right' caption='[[4b5r]], [[Resolution|resolution]] 2.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4b5r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B5R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B5R FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></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=4b5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b5r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b5r RCSB], [http://www.ebi.ac.uk/pdbsum/4b5r PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The k-turn is a widespread structural motif that introduces a tight kink into the helical axis of double-stranded RNA. The adenine bases of consecutive G*A pairs are directed toward the minor groove of the opposing helix, hydrogen bonding in a typical A-minor interaction. We show here that the available structures of k-turns divide into two classes, depending on whether N3 or N1 of the adenine at the 2b position accepts a hydrogen bond from the O2' at the -1n position. There is a coordinated structural change involving a number of hydrogen bonds between the two classes. We show here that Kt-7 can adopt either the N3 or N1 structures depending on environment. While it has the N1 structure in the ribosome, on engineering it into the SAM-I riboswitch, it changes to the N3 structure, resulting in a significant alteration in the trajectory of the helical arms. | |||
The plasticity of a structural motif in RNA: Structural polymorphism of a kink turn as a function of its environment.,Daldrop P, Lilley DM RNA. 2013 Jan 16. PMID:23325110<ref>PMID:23325110</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Riboswitch|Riboswitch]] | |||
== | == References == | ||
[[ | <references/> | ||
[[Category: Daldrop, P | __TOC__ | ||
[[Category: Lilley, D M.J | </StructureSection> | ||
[[Category: Daldrop, P]] | |||
[[Category: Lilley, D M.J]] | |||
[[Category: K-turn]] | [[Category: K-turn]] | ||
[[Category: Riboswitch]] | [[Category: Riboswitch]] | ||
[[Category: Rna]] | [[Category: Rna]] | ||
Revision as of 20:10, 9 December 2014
SAM-I riboswitch bearing the H. marismortui K-t-7SAM-I riboswitch bearing the H. marismortui K-t-7
Structural highlights
Publication Abstract from PubMedThe k-turn is a widespread structural motif that introduces a tight kink into the helical axis of double-stranded RNA. The adenine bases of consecutive G*A pairs are directed toward the minor groove of the opposing helix, hydrogen bonding in a typical A-minor interaction. We show here that the available structures of k-turns divide into two classes, depending on whether N3 or N1 of the adenine at the 2b position accepts a hydrogen bond from the O2' at the -1n position. There is a coordinated structural change involving a number of hydrogen bonds between the two classes. We show here that Kt-7 can adopt either the N3 or N1 structures depending on environment. While it has the N1 structure in the ribosome, on engineering it into the SAM-I riboswitch, it changes to the N3 structure, resulting in a significant alteration in the trajectory of the helical arms. The plasticity of a structural motif in RNA: Structural polymorphism of a kink turn as a function of its environment.,Daldrop P, Lilley DM RNA. 2013 Jan 16. PMID:23325110[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||