2M24
NMR solution structure of the d3'-hairpin including the exon binding site 1 (EBS1) of the group II intron Sc.ai5gamma
Replaces: 2K63Summary for 2M24
Entry DOI | 10.2210/pdb2m24/pdb |
Related | 2K63 2K64 2K65 2K66 2M1V 2M23 |
NMR Information | BMRB: 18894 |
Descriptor | RNA (29-MER) (1 entity in total) |
Functional Keywords | group ii intron, ribozyme, splicing, ebs1, hairpin, rna |
Biological source | Saccharomyces cerevisiae |
Total number of polymer chains | 1 |
Total formula weight | 9301.55 |
Authors | Kruschel, D.,Skilandat, M.,Sigel, R.K.O. (deposition date: 2012-12-12, release date: 2013-12-18, Last modification date: 2024-05-01) |
Primary citation | Kruschel, D.,Skilandat, M.,Sigel, R.K. NMR structure of the 5' splice site in the group IIB intron Sc.ai5 gamma--conformational requirements for exon-intron recognition. Rna, 20:295-307, 2014 Cited by PubMed Abstract: A crucial step of the self-splicing reaction of group II intron ribozymes is the recognition of the 5' exon by the intron. This recognition is achieved by two regions in domain 1 of the intron, the exon-binding sites EBS1 and EBS2 forming base pairs with the intron-binding sites IBS1 and IBS2 located at the end of the 5' exon. The complementarity of the EBS1•IBS1 contact is most important for ensuring site-specific cleavage of the phosphodiester bond between the 5' exon and the intron. Here, we present the NMR solution structures of the d3' hairpin including EBS1 free in solution and bound to the IBS1 7-mer. In the unbound state, EBS1 is part of a flexible 11-nucleotide (nt) loop. Binding of IBS1 restructures and freezes the entire loop region. Mg(2+) ions are bound near the termini of the EBS1•IBS1 helix, stabilizing the interaction. Formation of the 7-bp EBS1•IBS1 helix within a loop of only 11 nt forces the loop backbone to form a sharp turn opposite of the splice site, thereby presenting the scissile phosphate in a position that is structurally unique. PubMed: 24448450DOI: 10.1261/rna.041137.113 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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