Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5IW7

Crystal structure of yeast Tsr1, a pre-40S ribosome synthesis factor

Summary for 5IW7
Entry DOI10.2210/pdb5iw7/pdb
EMDB information1922 1926 1927
DescriptorRibosome biogenesis protein TSR1,Ribosome biogenesis protein TSR1 (1 entity in total)
Functional Keywordstranslational gtpase ribosome synthesis, translation
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
More
Cellular locationCytoplasm: Q07381
Total number of polymer chains4
Total formula weight324075.97
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 citationMcCaughan, 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: 27250689
DOI: 10.1038/ncomms11789
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.6 Å)
Structure validation

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon