8V87
60S ribosome biogenesis intermediate (Dbp10 post-catalytic structure - Overall map)
This is a non-PDB format compatible entry.
Summary for 8V87
Entry DOI | 10.2210/pdb8v87/pdb |
Related | 8V83 8V84 8V85 |
EMDB information | 43027 |
Descriptor | 25S ribosomal RNA, ATP-dependent RNA helicase HAS1, 60S ribosomal protein L6-A, ... (61 entities in total) |
Functional Keywords | ribosome biogenesis, intermediate dead-box atpase, ribosome-rna complex, ribosome/rna |
Biological source | Saccharomyces cerevisiae BY4741 More |
Total number of polymer chains | 56 |
Total formula weight | 2997720.49 |
Authors | Cruz, V.E.,Weirich, C.S.,Peddada, N.,Erzberger, J.P. (deposition date: 2023-12-04, release date: 2024-05-01) |
Primary citation | Cruz, V.E.,Weirich, C.S.,Peddada, N.,Erzberger, J.P. The DEAD-box ATPase Dbp10/DDX54 initiates peptidyl transferase center formation during 60S ribosome biogenesis. Nat Commun, 15:3296-3296, 2024 Cited by PubMed Abstract: DEAD-box ATPases play crucial roles in guiding rRNA restructuring events during the biogenesis of large (60S) ribosomal subunits, but their precise molecular functions are currently unknown. In this study, we present cryo-EM reconstructions of nucleolar pre-60S intermediates that reveal an unexpected, alternate secondary structure within the nascent peptidyl-transferase-center (PTC). Our analysis of three sequential nucleolar pre-60S intermediates reveals that the DEAD-box ATPase Dbp10/DDX54 remodels this alternate base pairing and enables the formation of the rRNA junction that anchors the mature form of the universally conserved PTC A-loop. Post-catalysis, Dbp10 captures rRNA helix H61, initiating the concerted exchange of biogenesis factors during late nucleolar 60S maturation. Our findings show that Dbp10 activity is essential for the formation of the ribosome active site and reveal how this function is integrated with subsequent assembly steps to drive the biogenesis of the large ribosomal subunit. PubMed: 38632236DOI: 10.1038/s41467-024-47616-7 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.66 Å) |
Structure validation
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