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1l8v
From Proteopedia
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|PDB= 1l8v |SIZE=350|CAPTION= <scene name='initialview01'>1l8v</scene>, resolution 2.80Å | |PDB= 1l8v |SIZE=350|CAPTION= <scene name='initialview01'>1l8v</scene>, resolution 2.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<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.ebi.ac.uk/pdbsum/1l8v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l8v RCSB]</span> | ||
}} | }} | ||
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[[Category: Battle, D J.]] | [[Category: Battle, D J.]] | ||
[[Category: Doudna, J A.]] | [[Category: Doudna, J A.]] | ||
| - | [[Category: MG]] | ||
[[Category: a-minor]] | [[Category: a-minor]] | ||
[[Category: ribozyme domain]] | [[Category: ribozyme domain]] | ||
[[Category: rna]] | [[Category: rna]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:59:41 2008'' |
Revision as of 18:59, 30 March 2008
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| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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
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