6NQI
Prp8 RH domain from C. merolae
Summary for 6NQI
| Entry DOI | 10.2210/pdb6nqi/pdb |
| Descriptor | Pre-mRNA splicing factor PRP8, BETA-MERCAPTOETHANOL (2 entities in total) |
| Functional Keywords | spliceosome, rnase h, splicing |
| Biological source | Cyanidioschyzon merolae (strain 10D) (Red alga) |
| Total number of polymer chains | 2 |
| Total formula weight | 49787.42 |
| Authors | Garside, E.L.,MacMillan, A.M. (deposition date: 2019-01-21, release date: 2019-05-22, Last modification date: 2023-10-11) |
| Primary citation | Garside, E.L.,Whelan, T.A.,Stark, M.R.,Rader, S.D.,Fast, N.M.,MacMillan, A.M. Prp8 in a Reduced Spliceosome Lacks a Conserved Toggle that Correlates with Splicing Complexity across Diverse Taxa. J.Mol.Biol., 431:2543-2553, 2019 Cited by PubMed Abstract: Conformational rearrangements are critical to regulating the assembly and activity of the spliceosome. The spliceosomal protein Prp8 undergoes multiple conformational changes during the course of spliceosome assembly, activation, and catalytic activity. Most of these rearrangements of Prp8 involve the disposition of the C-terminal Jab-MPN and RH domains with respect to the core of Prp8. Here we use x-ray structural analysis to show that a previously characterized and highly conserved β-hairpin structure in the RH domain that acts as a toggle in the spliceosome is absent in Prp8 from the reduced spliceosome of the red alga Cyanidioschyzon merolae. Using comparative sequence analysis, we show that the presence or absence of this hairpin corresponds to the presence or absence of protein partners that interact with this hairpin as observed by x-ray and cryo-EM studies. The presence of the toggle correlates with increasing intron number suggesting a role in the regulation of splicing. PubMed: 31078556DOI: 10.1016/j.jmb.2019.04.047 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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