5JNB
structure of GLD-2/RNP-8 complex
Summary for 5JNB
| Entry DOI | 10.2210/pdb5jnb/pdb |
| Descriptor | Poly(A) RNA polymerase gld-2, RNP (RRM RNA binding domain) containing, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | translational control, nucleotidyltransferase poly(a), polymerase, rna binding, c. elegans germline development, transferase |
| Biological source | Caenorhabditis elegans More |
| Cellular location | Cytoplasm : O17087 |
| Total number of polymer chains | 8 |
| Total formula weight | 189732.41 |
| Authors | Nakel, K.,Bonneau, F.,Basquin, C.,Eckmann, C.R.,Conti, E. (deposition date: 2016-04-29, release date: 2016-06-22, Last modification date: 2024-01-10) |
| Primary citation | Nakel, K.,Bonneau, F.,Basquin, C.,Habermann, B.,Eckmann, C.R.,Conti, E. Structural basis for the antagonistic roles of RNP-8 and GLD-3 in GLD-2 poly(A)-polymerase activity. Rna, 22:1139-1145, 2016 Cited by PubMed Abstract: Cytoplasmic polyadenylation drives the translational activation of specific mRNAs in early metazoan development and is performed by distinct complexes that share the same catalytic poly(A)-polymerase subunit, GLD-2. The activity and specificity of GLD-2 depend on its binding partners. In Caenorhabditis elegans, GLD-2 promotes spermatogenesis when bound to GLD-3 and oogenesis when bound to RNP-8. GLD-3 and RNP-8 antagonize each other and compete for GLD-2 binding. Following up on our previous mechanistic studies of GLD-2-GLD-3, we report here the 2.5 Å resolution structure and biochemical characterization of a GLD-2-RNP-8 core complex. In the structure, RNP-8 embraces the poly(A)-polymerase, docking onto several conserved hydrophobic hotspots present on the GLD-2 surface. RNP-8 stabilizes GLD-2 and indirectly stimulates polyadenylation. RNP-8 has a different amino-acid sequence and structure as compared to GLD-3. Yet, it binds the same surfaces of GLD-2 by forming alternative interactions, rationalizing the remarkable versatility of GLD-2 complexes. PubMed: 27288313DOI: 10.1261/rna.056598.116 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.486 Å) |
Structure validation
Download full validation report
