1l8v: Difference between revisions
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==Crystal Structure of a Mutant (C109G,G212C) P4-P6 Domain of the Group I Intron from Tetrahymena Thermophilia== | |||
<StructureSection load='1l8v' size='340' side='right' caption='[[1l8v]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1l8v]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L8V FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1l8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l8v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1l8v RCSB], [http://www.ebi.ac.uk/pdbsum/1l8v PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Functional RNAs often form compact structures characterized by closely packed helices. Crystallographic analysis of several large RNAs revealed a prevalent interaction in which unpaired adenosine residues dock into the minor groove of a receptor helix. This A-minor motif, potentially the most important element responsible for global RNA architecture, has also been suggested to contribute to the fidelity of protein synthesis by discriminating against near-cognate tRNAs on the ribosome. The specificity of A-minor interactions is fundamental to RNA tertiary structure formation, as well as to their proposed role in translational accuracy. To investigate A-minor motif specificity, we analyzed mutations in an A-minor interaction within the Tetrahymena group I self-splicing intron. Thermodynamic and x-ray crystallographic results show that the A-minor interaction strongly prefers canonical base pairs over base mismatches in the receptor helix, enabling RNA interhelical packing through specific recognition of Watson-Crick minor groove geometry. | |||
Specificity of RNA-RNA helix recognition.,Battle DJ, Doudna JA Proc Natl Acad Sci U S A. 2002 Sep 3;99(18):11676-81. Epub 2002 Aug 20. PMID:12189204<ref>PMID:12189204</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Group I intron|Group I intron]] | *[[Group I intron|Group I intron]] | ||
*[[Ribozyme|Ribozyme]] | *[[Ribozyme|Ribozyme]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: Battle, D J | </StructureSection> | ||
[[Category: Doudna, J A | [[Category: Battle, D J]] | ||
[[Category: Doudna, J A]] | |||
[[Category: A-minor]] | [[Category: A-minor]] | ||
[[Category: Ribozyme domain]] | [[Category: Ribozyme domain]] | ||
[[Category: Rna]] | [[Category: Rna]] | ||
Revision as of 14:07, 17 December 2014
Crystal Structure of a Mutant (C109G,G212C) P4-P6 Domain of the Group I Intron from Tetrahymena Thermophilia
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