1l8v
From Proteopedia
(New page: 200px<br /><applet load="1l8v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l8v, resolution 2.80Å" /> '''Crystal Structure of...) |
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| - | [[Image:1l8v.gif|left|200px]]<br /><applet load="1l8v" size=" | + | [[Image:1l8v.gif|left|200px]]<br /><applet load="1l8v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1l8v, resolution 2.80Å" /> | caption="1l8v, resolution 2.80Å" /> | ||
'''Crystal Structure of a Mutant (C109G,G212C) P4-P6 Domain of the Group I Intron from Tetrahymena Thermophilia'''<br /> | '''Crystal Structure of a Mutant (C109G,G212C) P4-P6 Domain of the Group I Intron from Tetrahymena Thermophilia'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Functional RNAs often form compact structures characterized by closely | + | 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== | ==About this Structure== | ||
| - | 1L8V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1L8V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8V OCA]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12189204 12189204] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12189204 12189204] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Battle, D | + | [[Category: Battle, D J.]] |
| - | [[Category: Doudna, J | + | [[Category: Doudna, J A.]] |
[[Category: MG]] | [[Category: MG]] | ||
[[Category: a-minor]] | [[Category: a-minor]] | ||
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[[Category: rna]] | [[Category: rna]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:35 2008'' |
Revision as of 11:42, 21 February 2008
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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 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 Thu Feb 21 13:42:35 2008
Categories: Protein complex | Battle, D J. | Doudna, J A. | MG | A-minor | Ribozyme domain | Rna
