7NAD
State E2 nucleolar 60S ribosomal biogenesis intermediate - Spb4 local refinement model
Summary for 7NAD
Entry DOI | 10.2210/pdb7nad/pdb |
Related | 7NAC |
EMDB information | 24269 24270 |
Descriptor | 25S rRNA, 60S ribosomal protein L22-A, 60S ribosomal protein L23-A, ... (27 entities in total) |
Functional Keywords | ribosome biogenesis, dead-box atpases, methyltransferase, nucleolus, ribosome |
Biological source | Saccharomyces cerevisiae BY4741 More |
Total number of polymer chains | 26 |
Total formula weight | 1068092.46 |
Authors | Cruz, V.E.,Sekulski, K.,Peddada, N.,Erzberger, J.P. (deposition date: 2021-06-21, release date: 2022-11-09, Last modification date: 2024-06-05) |
Primary citation | Cruz, V.E.,Sekulski, K.,Peddada, N.,Sailer, C.,Balasubramanian, S.,Weirich, C.S.,Stengel, F.,Erzberger, J.P. Sequence-specific remodeling of a topologically complex RNP substrate by Spb4. Nat.Struct.Mol.Biol., 29:1228-1238, 2022 Cited by PubMed Abstract: DEAD-box ATPases are ubiquitous enzymes essential in all aspects of RNA biology. However, the limited in vitro catalytic activities described for these enzymes are at odds with their complex cellular roles, most notably in driving large-scale RNA remodeling steps during the assembly of ribonucleoproteins (RNPs). We describe cryo-EM structures of 60S ribosomal biogenesis intermediates that reveal how context-specific RNA unwinding by the DEAD-box ATPase Spb4 results in extensive, sequence-specific remodeling of rRNA secondary structure. Multiple cis and trans interactions stabilize Spb4 in a post-catalytic, high-energy intermediate that drives the organization of the three-way junction at the base of rRNA domain IV. This mechanism explains how limited strand separation by DEAD-box ATPases is leveraged to provide non-equilibrium directionality and ensure efficient and accurate RNP assembly. PubMed: 36482249DOI: 10.1038/s41594-022-00874-9 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.04 Å) |
Structure validation
Download full validation report