5IW7
Crystal structure of yeast Tsr1, a pre-40S ribosome synthesis factor
Summary for 5IW7
Entry DOI | 10.2210/pdb5iw7/pdb |
EMDB information | 1922 1926 1927 |
Descriptor | Ribosome biogenesis protein TSR1,Ribosome biogenesis protein TSR1 (1 entity in total) |
Functional Keywords | translational gtpase ribosome synthesis, translation |
Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
Cellular location | Cytoplasm: Q07381 |
Total number of polymer chains | 4 |
Total formula weight | 324075.97 |
Authors | McCaughan, U.M.,Jayachandran, U.,Cook, A.G. (deposition date: 2016-03-22, release date: 2016-06-15, Last modification date: 2024-05-08) |
Primary citation | McCaughan, U.M.,Jayachandran, U.,Shchepachev, V.,Chen, Z.A.,Rappsilber, J.,Tollervey, D.,Cook, A.G. Pre-40S ribosome biogenesis factor Tsr1 is an inactive structural mimic of translational GTPases. Nat Commun, 7:11789-11789, 2016 Cited by PubMed Abstract: Budding yeast Tsr1 is a ribosome biogenesis factor with sequence similarity to GTPases, which is essential for cytoplasmic steps in 40S subunit maturation. Here we present the crystal structure of Tsr1 at 3.6 Å. Tsr1 has a similar domain architecture to translational GTPases such as EF-Tu and the selenocysteine incorporation factor SelB. However, active site residues required for GTP binding and hydrolysis are absent, explaining the lack of enzymatic activity in previous analyses. Modelling of Tsr1 into cryo-electron microscopy maps of pre-40S particles shows that a highly acidic surface of Tsr1 is presented on the outside of pre-40S particles, potentially preventing premature binding to 60S subunits. Late pre-40S maturation also requires the GTPase eIF5B and the ATPase Rio1. The location of Tsr1 is predicted to block binding by both factors, strongly indicating that removal of Tsr1 is an essential step during cytoplasmic maturation of 40S ribosomal subunits. PubMed: 27250689DOI: 10.1038/ncomms11789 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.6 Å) |
Structure validation
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