4P9R
Speciation of a group I intron into a lariat capping ribozyme (Heavy atom derivative)
Summary for 4P9R
| Entry DOI | 10.2210/pdb4p9r/pdb |
| Related | 4P8Z 4P95 |
| Descriptor | RNA (189-MER), IRIDIUM HEXAMMINE ION, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | catalytic rna, lariat-capping ribozyme, branching reaction, lariat fold, rna |
| Biological source | Didymium iridis |
| Total number of polymer chains | 1 |
| Total formula weight | 64908.62 |
| Authors | Meyer, M.,Nielsen, H.,Olieric, V.,Roblin, P.,Johansen, S.D.,Westhof, E.,Masquida, B. (deposition date: 2014-04-04, release date: 2014-05-28, Last modification date: 2023-12-27) |
| Primary citation | Meyer, M.,Nielsen, H.,Olieric, V.,Roblin, P.,Johansen, S.D.,Westhof, E.,Masquida, B. Speciation of a group I intron into a lariat capping ribozyme. Proc.Natl.Acad.Sci.USA, 111:7659-7664, 2014 Cited by PubMed Abstract: The lariat-capping (LC) ribozyme is a natural ribozyme isolated from eukaryotic microorganisms. Despite apparent structural similarity to group I introns, the LC ribozyme catalyzes cleavage by a 2',5' branching reaction, leaving the 3' product with a 3-nt lariat cap that functionally substitutes for a conventional mRNA cap in the downstream pre-mRNA encoding a homing endonuclease. We describe the crystal structures of the precleavage and postcleavage LC ribozymes, which suggest that structural features inherited from group I ribozymes have undergone speciation due to profound changes in molecular selection pressure, ultimately giving rise to an original branching ribozyme family. The structures elucidate the role of key elements that regulate the activity of the LC ribozyme by conformational switching and suggest a mechanism by which the signal for branching is transmitted to the catalytic core. The structures also show how conserved interactions twist residues, forming the lariat to join chemical groups involved in branching. PubMed: 24821772DOI: 10.1073/pnas.1322248111 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.703 Å) |
Structure validation
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