4CV5
yeast NOT1 CN9BD-CAF40 complex
Summary for 4CV5
| Entry DOI | 10.2210/pdb4cv5/pdb |
| Descriptor | GENERAL NEGATIVE REGULATOR OF TRANSCRIPTION SUBUNIT 1, PROTEIN CAF40, HEXATANTALUM DODECABROMIDE (3 entities in total) |
| Functional Keywords | cell cycle |
| Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) More |
| Cellular location | Cytoplasm: P25655 Cytoplasm (Probable): P53829 |
| Total number of polymer chains | 4 |
| Total formula weight | 125332.56 |
| Authors | Basquin, J.,Conti, E. (deposition date: 2014-03-23, release date: 2014-05-07, Last modification date: 2024-05-08) |
| Primary citation | Mathys, H.,Basquin, J.,Ozgur, S.,Czarnocki-Cieciura, M.,Bonneau, F.,Aartse, A.,Dziembowski, A.,Nowotny, M.,Conti, E.,Filipowicz, W. Structural and Biochemical Insights to the Role of the Ccr4-not Complex and Ddx6 ATPase in Microrna Repression. Mol.Cell, 54:751-, 2014 Cited by PubMed Abstract: MicroRNAs (miRNAs) control gene expression by regulating mRNA translation and stability. The CCR4-NOT complex is a key effector of miRNA function acting downstream of GW182/TNRC6 proteins. We show that miRNA-mediated repression requires the central region of CNOT1, the scaffold protein of CCR4-NOT. A CNOT1 domain interacts with CNOT9, which in turn interacts with the silencing domain of TNRC6 in a tryptophan motif-dependent manner. These interactions are direct, as shown by the structure of a CNOT9-CNOT1 complex with bound tryptophan. Another domain of CNOT1 with an MIF4G fold recruits the DEAD-box ATPase DDX6, a known translational inhibitor. Structural and biochemical approaches revealed that CNOT1 modulates the conformation of DDX6 and stimulates ATPase activity. Structure-based mutations showed that the CNOT1 MIF4G-DDX6 interaction is important for miRNA-mediated repression. These findings provide insights into the repressive steps downstream of the GW182/TNRC6 proteins and the role of the CCR4-NOT complex in posttranscriptional regulation in general. PubMed: 24768538DOI: 10.1016/J.MOLCEL.2014.03.036 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.807 Å) |
Structure validation
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