1l8v
From Proteopedia
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Crystal Structure of a Mutant (C109G,G212C) P4-P6 Domain of the Group I Intron from Tetrahymena Thermophilia
Overview
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.
About this Structure
1L8V is a Protein complex structure of sequences from [1] with MG as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Nov 25 02:39:28 2007
Categories: Protein complex | Battle, D.J. | Doudna, J.A. | MG | A-minor | Ribozyme domain | Rna
