4V8T
Cryo-EM Structure of the 60S Ribosomal Subunit in Complex with Arx1 and Rei1
This is a non-PDB format compatible entry.
Summary for 4V8T
Entry DOI | 10.2210/pdb4v8t/pdb |
EMDB information | 2169 |
Descriptor | 60S ribosomal protein L2-A, 60S ribosomal protein L11-A, 60S RIBOSOMAL PROTEIN L12, ... (51 entities in total) |
Functional Keywords | large ribosomal subunit, ribosome biogenesis, ribosome maturation factor, ribosome |
Biological source | Saccharomyces cerevisiae S288C More |
Total number of polymer chains | 50 |
Total formula weight | 2101457.46 |
Authors | Greber, B.J.,Boehringer, D.,Montellese, C.,Ban, N. (deposition date: 2012-08-07, release date: 2014-07-09, Last modification date: 2024-05-08) |
Primary citation | Greber, B.J.,Boehringer, D.,Montellese, C.,Ban, N. Cryo-Em Structures of Arx1 and Maturation Factors Rei1 and Jjj1 Bound to the 60S Ribosomal Subunit Nat.Struct.Mol.Biol., 19:1228-, 2012 Cited by PubMed Abstract: Eukaryotic ribosome biogenesis requires many protein factors that facilitate the assembly, nuclear export and final maturation of 40S and 60S particles. We have biochemically characterized ribosomal complexes of the yeast 60S-biogenesis factor Arx1 and late-maturation factors Rei1 and Jjj1 and determined their cryo-EM structures. Arx1 was visualized bound to the 60S subunit together with Rei1, at 8.1-Å resolution, to reveal the molecular details of Arx1 binding whereby Arx1 arrests the eukaryotic-specific rRNA expansion segment 27 near the polypeptide tunnel exit. Rei1 and Jjj1, which have been implicated in Arx1 recycling, bind in the vicinity of Arx1 and form a network of interactions. We suggest that, in addition to the role of Arx1 during pre-60S nuclear export, the binding of Arx1 conformationally locks the pre-60S subunit and inhibits the premature association of nascent chain-processing factors to the polypeptide tunnel exit. PubMed: 23142985DOI: 10.1038/NSMB.2425 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (8.1 Å) |
Structure validation
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