5O1W
Structure of Nrd1 RNA binding domain
Summary for 5O1W
| Entry DOI | 10.2210/pdb5o1w/pdb |
| Descriptor | Protein NRD1, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | nrd1, rrm, rna-binding, transcription non-coding rnas, nrd1 complex, transcription |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Cellular location | Nucleus : P53617 |
| Total number of polymer chains | 1 |
| Total formula weight | 21357.99 |
| Authors | Franco-Echevarria, E.,Perez-Canadillas, J.M.,Gonzalez, B. (deposition date: 2017-05-19, release date: 2017-08-02, Last modification date: 2024-05-08) |
| Primary citation | Franco-Echevarria, E.,Gonzalez-Polo, N.,Zorrilla, S.,Martinez-Lumbreras, S.,Santiveri, C.M.,Campos-Olivas, R.,Sanchez, M.,Calvo, O.,Gonzalez, B.,Perez-Canadillas, J.M. The structure of transcription termination factor Nrd1 reveals an original mode for GUAA recognition. Nucleic Acids Res., 45:10293-10305, 2017 Cited by PubMed Abstract: Transcription termination of non-coding RNAs is regulated in yeast by a complex of three RNA binding proteins: Nrd1, Nab3 and Sen1. Nrd1 is central in this process by interacting with Rbp1 of RNA polymerase II, Trf4 of TRAMP and GUAA/G terminator sequences. We lack structural data for the last of these binding events. We determined the structures of Nrd1 RNA binding domain and its complexes with three GUAA-containing RNAs, characterized RNA binding energetics and tested rationally designed mutants in vivo. The Nrd1 structure shows an RRM domain fused with a second α/β domain that we name split domain (SD), because it is formed by two non-consecutive segments at each side of the RRM. The GUAA interacts with both domains and with a pocket of water molecules, trapped between the two stacking adenines and the SD. Comprehensive binding studies demonstrate for the first time that Nrd1 has a slight preference for GUAA over GUAG and genetic and functional studies suggest that Nrd1 RNA binding domain might play further roles in non-coding RNAs transcription termination. PubMed: 28973465DOI: 10.1093/nar/gkx685 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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