9FMS
Cryo-EM structure of S. cerevisiae Rai1-Rat1-Rtt103(252-273) complex.
Summary for 9FMS
| Entry DOI | 10.2210/pdb9fms/pdb |
| Related | 8Q6V 9EXS |
| EMDB information | 18199 50048 50566 |
| Descriptor | 5'-3' exoribonuclease 2, Regulator of Ty1 transposition protein 103, Decapping nuclease RAI1, ... (4 entities in total) |
| Functional Keywords | rai1 nuclease, rtt103 binding, structured, rna binding, rna binding protein |
| Biological source | Saccharomyces cerevisiae (brewer's yeast) More |
| Total number of polymer chains | 3 |
| Total formula weight | 163135.08 |
| Authors | Noskova, N.,Dikunova, A.,Stefl, R. (deposition date: 2024-06-07, release date: 2024-12-18, Last modification date: 2025-02-19) |
| Primary citation | Dikunova, A.,Noskova, N.,Overbeck, J.H.,Polak, M.,Stelzig, D.,Zapletal, D.,Kubicek, K.,Novacek, J.,Sprangers, R.,Stefl, R. Assembly of the Xrn2/Rat1-Rai1-Rtt103 termination complexes in mesophilic and thermophilic organisms. Structure, 33:300-, 2025 Cited by PubMed Abstract: The 5'-3' exoribonuclease Xrn2, known as Rat1 in yeasts, terminates mRNA transcription by RNA polymerase II (RNAPII). In the torpedo model of termination, the activity of Xrn2/Rat1 is enhanced by Rai1, which is recruited to the termination site by Rtt103, an adaptor protein binding to the RNAPII C-terminal domain (CTD). The overall architecture of the Xrn2/Rat1-Rai1-Rtt103 complex remains unknown. We combined structural biology methods to characterize the torpedo complex from Saccharomyces cerevisiae and Chaetomium thermophilum. Comparison of the structures from these organisms revealed a conserved protein core fold of the subunits, but significant variability in their interaction interfaces. We found that in the mesophile, Rtt103 utilizes an unstructured region to augment a Rai1 β-sheet, while in the thermophile Rtt103 binds to a C-terminal helix of Rai1 via its CTD-interacting domain with an α-helical fold. These different torpedo complex assemblies reflect adaptations to the environment and impact complex recruitment to RNAPII. PubMed: 39657659DOI: 10.1016/j.str.2024.11.010 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.65 Å) |
Structure validation
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