4R0D
Crystal structure of a eukaryotic group II intron lariat
Summary for 4R0D
| Entry DOI | 10.2210/pdb4r0d/pdb |
| Descriptor | GROUP IIB INTRON LARIAT, LIGATED EXONS, SPERMINE, ... (7 entities in total) |
| Functional Keywords | lariat, ribozyme, 2'-5' phosphodiester, rna |
| Biological source | Pylaiella littoralis (brown algae) More |
| Total number of polymer chains | 2 |
| Total formula weight | 221496.04 |
| Authors | Robart, A.R.,Chan, R.T.,Peters, J.K.,Rajashankar, K.R.,Toor, N. (deposition date: 2014-07-30, release date: 2014-10-01, Last modification date: 2024-02-28) |
| Primary citation | Robart, A.R.,Chan, R.T.,Peters, J.K.,Rajashankar, K.R.,Toor, N. Crystal structure of a eukaryotic group II intron lariat. Nature, 514:193-197, 2014 Cited by PubMed Abstract: The formation of branched lariat RNA is an evolutionarily conserved feature of splicing reactions for both group II and spliceosomal introns. The lariat is important for the fidelity of 5' splice-site selection and consists of a 2'-5' phosphodiester bond between a bulged adenosine and the 5' end of the intron. To gain insight into this ubiquitous intramolecular linkage, we determined the crystal structure of a eukaryotic group IIB intron in the lariat form at 3.7 Å. This revealed that two tandem tetraloop-receptor interactions, η-η' and π-π', place domain VI in the core to position the lariat bond in the post-catalytic state. On the basis of structural and biochemical data, we propose that π-π' is a dynamic interaction that mediates the transition between the two steps of splicing, with η-η' serving an ancillary role. The structure also reveals a four-magnesium-ion cluster involved in both catalysis and positioning of the 5' end. Given the evolutionary relationship between group II and nuclear introns, it is likely that this active site configuration exists in the spliceosome as well. PubMed: 25252982DOI: 10.1038/nature13790 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.676 Å) |
Structure validation
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