5FCJ

Structure of the anisomycin-containing uL3 W255C mutant 80S yeast ribosome

This is a non-PDB format compatible entry.

Summary for 5FCJ

• Entry DOI: 10.2210/pdb5fcj/pdb
• Descriptor: 18S ribosomal RNA, 40S ribosomal protein S8-A, 40S ribosomal protein S9-A, ... (87 entities in total)
• Functional Keywords: ribosome, ul3 mutant, anisomycin
• Biological source: Saccharomyces cerevisiae S288c; More
• Cellular location: Cytoplasm : P0CX39 O13516 P48589 P05756 P06367 Q01855 P32905 P0CX51 P02407 P0CX55 P07280 P38701 P0C0V8 P0C0W1 P0CX29 P0CX31 Q3E792 P33442 P39939 P35997 Q3E7X9 P41057 P0CX33 P38011 P25443 P0CX45 P14126 P10664 P26321 Q02326 P05737 P17076 P05738 P05750 P41805 P0C0W9 Q12690 P36105 P05748 P26784 P05740 P0CX49 P0CX82 P0CX23 P0CX35 Q02753 P05749 P0CX41 P04449 P04456 P05743 P0C2H6 P02406 P05747 P14120 P26783 P0C2H8 P38061 P05744 P87262 P0CX84 P05745 P49166 P49167 P04650 P0CX37 P0CX86 P0CX27 P0CX25 P05317 P26786; Ubiquitin: Cytoplasm . 40S ribosomal protein S31: Cytoplasm : P05759; Ubiquitin: Cytoplasm . 60S ribosomal protein L40-A: Cytoplasm : P0CH08
• Total number of polymer chains: 162
• Total formula weight: 6565290.54

Authors

Mailliot, J.,Garreau de Loubresse, N.,Yusupova, G.,Dinman, J.D.,Yusupov, M. (deposition date: 2015-12-15, release date: 2016-05-11, Last modification date: 2024-01-10)

Primary citation

Mailliot, J.,Garreau de Loubresse, N.,Yusupova, G.,Meskauskas, A.,Dinman, J.D.,Yusupov, M.
Crystal Structures of the uL3 Mutant Ribosome: Illustration of the Importance of Ribosomal Proteins for Translation Efficiency.
J.Mol.Biol., 428:2195-2202, 2016

PubMed Abstract: The ribosome has been described as a ribozyme in which ribosomal RNA is responsible for peptidyl-transferase reaction catalysis. The W255C mutation of the universally conserved ribosomal protein uL3 has diverse effects on ribosome function (e.g., increased affinities for transfer RNAs, decreased rates of peptidyl-transfer), and cells harboring this mutation are resistant to peptidyl-transferase inhibitors (e.g., anisomycin). These observations beg the question of how a single amino acid mutation may have such wide ranging consequences. Here, we report the structure of the vacant yeast uL3 W255C mutant ribosome by X-ray crystallography, showing a disruption of the A-site side of the peptidyl-transferase center (PTC). An additional X-ray crystallographic structure of the anisomycin-containing mutant ribosome shows that high concentrations of this inhibitor restore a "WT-like" configuration to this region of the PTC, providing insight into the resistance mechanism of the mutant. Globally, our data demonstrate that ribosomal protein uL3 is structurally essential to ensure an optimal and catalytically efficient organization of the PTC, highlighting the importance of proteins in the RNA-centered ribosome.

PubMed: 26906928
DOI: 10.1016/j.jmb.2016.02.013

Experimental method

X-RAY DIFFRACTION (3.1 Å)