1L8V

Crystal Structure of a Mutant (C109G,G212C) P4-P6 Domain of the Group I Intron from Tetrahymena Thermophilia

Summary for 1L8V

• Entry DOI: 10.2210/pdb1l8v/pdb
• Descriptor: P4-P6 RNA ribozyme domain, MAGNESIUM ION (3 entities in total)
• Functional Keywords: rna, ribozyme domain, a-minor
• Total number of polymer chains: 2
• Total formula weight: 101687.28

Authors

Battle, D.J.,Doudna, J.A. (deposition date: 2002-03-21, release date: 2002-08-23, Last modification date: 2023-08-16)

Primary citation

Battle, D.J.,Doudna, J.A.
Specificity of RNA-RNA Helix Recognition
Proc.Natl.Acad.Sci.USA, 99:11676-11681, 2002

PubMed Abstract: 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.

PubMed: 12189204
DOI: 10.1073/pnas.182221799

Experimental method

X-RAY DIFFRACTION (2.8 Å)