7MQJ
Dhr1 Helicase Core
Summary for 7MQJ
| Entry DOI | 10.2210/pdb7mqj/pdb |
| Descriptor | Probable ATP-dependent RNA helicase DHR1, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | helicase, ribosome assembly, hydrolase |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 91244.67 |
| Authors | Miller, L.,Chaker-Margot, M.,Klinge, S. (deposition date: 2021-05-05, release date: 2021-09-22, Last modification date: 2023-10-18) |
| Primary citation | Singh, S.,Vanden Broeck, A.,Miller, L.,Chaker-Margot, M.,Klinge, S. Nucleolar maturation of the human small subunit processome. Science, 373:eabj5338-eabj5338, 2021 Cited by PubMed Abstract: The human small subunit processome mediates early maturation of the small ribosomal subunit by coupling RNA folding to subsequent RNA cleavage and processing steps. We report the high-resolution cryo–electron microscopy structures of maturing human small subunit (SSU) processomes at resolutions of 2.7 to 3.9 angstroms. These structures reveal the molecular mechanisms that enable crucial progressions during SSU processome maturation. RNA folding states within these particles are communicated to and coordinated with key enzymes that drive irreversible steps such as targeted exosome-mediated RNA degradation, protein-guided site-specific endonucleolytic RNA cleavage, and tightly controlled RNA unwinding. These conserved mechanisms highlight the SSU processome’s impressive structural plasticity, which endows this 4.5-megadalton nucleolar assembly with the distinctive ability to mature the small ribosomal subunit from within. PubMed: 34516797DOI: 10.1126/science.abj5338 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.23 Å) |
Structure validation
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