6ZQC
Cryo-EM structure of the 90S pre-ribosome from Saccharomyces cerevisiae, state Pre-A1
This is a non-PDB format compatible entry.
Summary for 6ZQC
Entry DOI | 10.2210/pdb6zqc/pdb |
EMDB information | 11359 |
Descriptor | rRNA 2'-O-methyltransferase fibrillarin, U3 small nucleolar RNA-associated protein 7, U3 small nucleolar RNA-associated protein 8, ... (70 entities in total) |
Functional Keywords | ribosome, 90s pre-ribosome, 40s pre-ribosome, a1 cleavage, dhr1 |
Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
Total number of polymer chains | 71 |
Total formula weight | 4866244.50 |
Authors | Cheng, J.,Lau, B.,Venuta, G.L.,Berninghausen, O.,Hurt, E.,Beckmann, R. (deposition date: 2020-07-09, release date: 2020-09-23, Last modification date: 2024-05-01) |
Primary citation | Cheng, J.,Lau, B.,La Venuta, G.,Ameismeier, M.,Berninghausen, O.,Hurt, E.,Beckmann, R. 90 S pre-ribosome transformation into the primordial 40 S subunit. Science, 369:1470-1476, 2020 Cited by PubMed Abstract: Production of small ribosomal subunits initially requires the formation of a 90 precursor followed by an enigmatic process of restructuring into the primordial pre-40 subunit. We elucidate this process by biochemical and cryo-electron microscopy analysis of intermediates along this pathway in yeast. First, the remodeling RNA helicase Dhr1 engages the 90 pre-ribosome, followed by Utp24 endonuclease-driven RNA cleavage at site A, thereby separating the 5'-external transcribed spacer (ETS) from 18 ribosomal RNA. Next, the 5'-ETS and 90 assembly factors become dislodged, but this occurs sequentially, not en bloc. Eventually, the primordial pre-40 emerges, still retaining some 90 factors including Dhr1, now ready to unwind the final small nucleolar U3-18 RNA hybrid. Our data shed light on the elusive 90 to pre-40 transition and clarify the principles of assembly and remodeling of large ribonucleoproteins. PubMed: 32943521DOI: 10.1126/science.abb4119 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
Download full validation report