5MDU
Structure of the RNA recognition motif (RRM) of Seb1 from S. pombe.
Summary for 5MDU
Entry DOI | 10.2210/pdb5mdu/pdb |
Related | 5MDT |
Descriptor | Rpb7-binding protein seb1, CHLORIDE ION, SODIUM ION, ... (5 entities in total) |
Functional Keywords | rna recognition motif (rrm), s. pombe, transcription termination, rna binding, transcription |
Biological source | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
Cellular location | Nucleus : Q9UTE3 |
Total number of polymer chains | 1 |
Total formula weight | 17643.45 |
Authors | Wittmann, S.,Renner, M.,El Omari, K.,Adams, O.,Vasiljeva, L.,Grimes, J. (deposition date: 2016-11-13, release date: 2017-04-12, Last modification date: 2024-05-08) |
Primary citation | Wittmann, S.,Renner, M.,Watts, B.R.,Adams, O.,Huseyin, M.,Baejen, C.,El Omari, K.,Kilchert, C.,Heo, D.H.,Kecman, T.,Cramer, P.,Grimes, J.M.,Vasiljeva, L. The conserved protein Seb1 drives transcription termination by binding RNA polymerase II and nascent RNA. Nat Commun, 8:14861-14861, 2017 Cited by PubMed Abstract: Termination of RNA polymerase II (Pol II) transcription is an important step in the transcription cycle, which involves the dislodgement of polymerase from DNA, leading to release of a functional transcript. Recent studies have identified the key players required for this process and showed that a common feature of these proteins is a conserved domain that interacts with the phosphorylated C-terminus of Pol II (CTD-interacting domain, CID). However, the mechanism by which transcription termination is achieved is not understood. Using genome-wide methods, here we show that the fission yeast CID-protein Seb1 is essential for termination of protein-coding and non-coding genes through interaction with S2-phosphorylated Pol II and nascent RNA. Furthermore, we present the crystal structures of the Seb1 CTD- and RNA-binding modules. Unexpectedly, the latter reveals an intertwined two-domain arrangement of a canonical RRM and second domain. These results provide important insights into the mechanism underlying eukaryotic transcription termination. PubMed: 28367989DOI: 10.1038/ncomms14861 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.02 Å) |
Structure validation
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