6NX5
Crystal structure of the RRM domain of S. pombe Puf1 in the P21 space group
Summary for 6NX5
| Entry DOI | 10.2210/pdb6nx5/pdb |
| Related | 6NWW |
| Descriptor | Pumilio domain-containing protein C56F2.08c, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | the rrm domain, rna binding protein |
| Biological source | Schizosaccharomyces pombe (Fission yeast) |
| Total number of polymer chains | 4 |
| Total formula weight | 35571.73 |
| Authors | Qiu, C.,Hall, T.M.T. (deposition date: 2019-02-08, release date: 2019-07-03, Last modification date: 2024-03-13) |
| Primary citation | Qiu, C.,Dutcher, R.C.,Porter, D.F.,Arava, Y.,Wickens, M.,Hall, T.M.T. Distinct RNA-binding modules in a single PUF protein cooperate to determine RNA specificity. Nucleic Acids Res., 47:8770-8784, 2019 Cited by PubMed Abstract: PUF proteins, named for Drosophila Pumilio (PUM) and Caenorhabditis elegans fem-3-binding factor (FBF), recognize specific sequences in the mRNAs they bind and control. RNA binding by classical PUF proteins is mediated by a characteristic PUM homology domain (PUM-HD). The Puf1 and Puf2 proteins possess a distinct architecture and comprise a highly conserved subfamily among fungal species. Puf1/Puf2 proteins contain two types of RNA-binding domain: a divergent PUM-HD and an RNA recognition motif (RRM). They recognize RNAs containing UAAU motifs, often in clusters. Here, we report a crystal structure of the PUM-HD of a fungal Puf1 in complex with a dual UAAU motif RNA. Each of the two UAAU tetranucleotides are bound by a Puf1 PUM-HD forming a 2:1 protein-to-RNA complex. We also determined crystal structures of the Puf1 RRM domain that identified a dimerization interface. The PUM-HD and RRM domains act in concert to determine RNA-binding specificity: the PUM-HD dictates binding to UAAU, and dimerization of the RRM domain favors binding to dual UAAU motifs rather than a single UAAU. Cooperative action of the RRM and PUM-HD identifies a new mechanism by which multiple RNA-binding modules in a single protein collaborate to create a unique RNA-binding specificity. PubMed: 31294800DOI: 10.1093/nar/gkz583 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.554 Å) |
Structure validation
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