6H0R
X-ray structure of SRS2 fragment of Rgs4 3' UTR
Summary for 6H0R
| Entry DOI | 10.2210/pdb6h0r/pdb |
| Descriptor | SRS2 fragment of Rgs4 3' UTR, RNA (31-MER), BARIUM ION, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | rna, rgs4 |
| Biological source | Rattus norvegicus (Norway rat) |
| Total number of polymer chains | 2 |
| Total formula weight | 21471.92 |
| Authors | Heber, S.,Janowski, R.,Niessing, D. (deposition date: 2018-07-10, release date: 2019-04-17, Last modification date: 2024-05-15) |
| Primary citation | Heber, S.,Gaspar, I.,Tants, J.N.,Gunther, J.,Moya, S.M.F.,Janowski, R.,Ephrussi, A.,Sattler, M.,Niessing, D. Staufen2-mediated RNA recognition and localization requires combinatorial action of multiple domains. Nat Commun, 10:1659-1659, 2019 Cited by PubMed Abstract: Throughout metazoans, Staufen (Stau) proteins are core factors of mRNA localization particles. They consist of three to four double-stranded RNA binding domains (dsRBDs) and a C-terminal dsRBD-like domain. Mouse Staufen2 (mStau2)-like Drosophila Stau (dmStau) contains four dsRBDs. Existing data suggest that only dsRBDs 3-4 are necessary and sufficient for mRNA binding. Here, we show that dsRBDs 1 and 2 of mStau2 bind RNA with similar affinities and kinetics as dsRBDs 3 and 4. While RNA binding by these tandem domains is transient, all four dsRBDs recognize their target RNAs with high stability. Rescue experiments in Drosophila oocytes demonstrate that mStau2 partially rescues dmStau-dependent mRNA localization. In contrast, a rescue with mStau2 bearing RNA-binding mutations in dsRBD1-2 fails, confirming the physiological relevance of our findings. In summary, our data show that the dsRBDs 1-2 play essential roles in the mRNA recognition and function of Stau-family proteins of different species. PubMed: 30971701DOI: 10.1038/s41467-019-09655-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.73 Å) |
Structure validation
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