Summary for 6OR5
| Entry DOI | 10.2210/pdb6or5/pdb |
| EMDB information | 9032 9033 9034 9035 9036 |
| Descriptor | Midasin, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (2 entities in total) |
| Functional Keywords | ribosome biogenesis, aaa protein, mechanochemical enzyme, ribosome assembly factor, motor protein |
| Biological source | Schizosaccharomyces pombe (Fission yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 540912.10 |
| Authors | Chen, Z.,Suzuki, H.,Wang, A.C.,DiMaio, F.,Walz, T.,Kapoor, T.M. (deposition date: 2019-04-29, release date: 2019-05-29, Last modification date: 2024-03-13) |
| Primary citation | Chen, Z.,Suzuki, H.,Kobayashi, Y.,Wang, A.C.,DiMaio, F.,Kawashima, S.A.,Walz, T.,Kapoor, T.M. Structural Insights into Mdn1, an Essential AAA Protein Required for Ribosome Biogenesis. Cell, 175:822-834.e18, 2018 Cited by PubMed Abstract: Mdn1 is an essential AAA (ATPase associated with various activities) protein that removes assembly factors from distinct precursors of the ribosomal 60S subunit. However, Mdn1's large size (∼5,000 amino acid [aa]) and its limited homology to other well-studied proteins have restricted our understanding of its remodeling function. Here, we present structures for S. pombe Mdn1 in the presence of AMPPNP at up to ∼4 Å or ATP plus Rbin-1, a chemical inhibitor, at ∼8 Å resolution. These data reveal that Mdn1's MIDAS domain is tethered to its ring-shaped AAA domain through an ∼20 nm long structured linker and a flexible ∼500 aa Asp/Glu-rich motif. We find that the MIDAS domain, which also binds other ribosome-assembly factors, docks onto the AAA ring in a nucleotide state-specific manner. Together, our findings reveal how conformational changes in the AAA ring can be directly transmitted to the MIDAS domain and thereby drive the targeted release of assembly factors from ribosomal 60S-subunit precursors. PubMed: 30318141DOI: 10.1016/j.cell.2018.09.015 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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