5J01
Structure of the lariat form of a chimeric derivative of the Oceanobacillus iheyensis group II intron in the presence of NH4+ and MG2+.
Summary for 5J01
| Entry DOI | 10.2210/pdb5j01/pdb |
| Descriptor | group II intron lariat, MAGNESIUM ION, AMMONIUM ION, ... (4 entities in total) |
| Functional Keywords | group ii intron, lariat, 2'-5' phosphodiester bond, ribozyme, rna catalysis, self-splicing, rna |
| Biological source | Oceanobacillus iheyensis |
| Total number of polymer chains | 1 |
| Total formula weight | 136698.30 |
| Authors | Costa, M.,Walbott, H.,Monachello, D.,Westhof, E.,Michel, F. (deposition date: 2016-03-26, release date: 2016-12-14, Last modification date: 2024-01-10) |
| Primary citation | Costa, M.,Walbott, H.,Monachello, D.,Westhof, E.,Michel, F. Crystal structures of a group II intron lariat primed for reverse splicing. Science, 354:-, 2016 Cited by PubMed Abstract: The 2'-5' branch of nuclear premessenger introns is believed to have been inherited from self-splicing group II introns, which are retrotransposons of bacterial origin. Our crystal structures at 3.4 and 3.5 angstrom of an excised group II intron in branched ("lariat") form show that the 2'-5' branch organizes a network of active-site tertiary interactions that position the intron terminal 3'-hydroxyl group into a configuration poised to initiate reverse splicing, the first step in retrotransposition. Moreover, the branchpoint and flanking helices must undergo a base-pairing switch after branch formation. A group II-based model of the active site of the nuclear splicing machinery (the spliceosome) is proposed. The crucial role of the lariat conformation in active-site assembly and catalysis explains its prevalence in modern splicing. PubMed: 27934709DOI: 10.1126/science.aaf9258 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.39 Å) |
Structure validation
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