Summary for 4V95
| Entry DOI | 10.2210/pdb4v95/pdb |
| Descriptor | 16S Ribosomal RNA, 30S Ribosomal Protein S10, 30S Ribosomal Protein S11, ... (58 entities in total) |
| Functional Keywords | ribosome, yaej, ribosome stalling, ribosome rescue, rescue factor, alternative rescue factor, arfb, release factor, rescue of stalled ribosomes |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 109 |
| Total formula weight | 4470834.22 |
| Authors | Gagnon, M.G.,Seetharaman, S.V.,Bulkley, D.P.,Steitz, T.A. (deposition date: 2012-01-27, release date: 2014-07-09, Last modification date: 2024-11-06) |
| Primary citation | Gagnon, M.G.,Seetharaman, S.V.,Bulkley, D.,Steitz, T.A. Structural basis for the rescue of stalled ribosomes: structure of YaeJ bound to the ribosome. Science, 335:1370-1372, 2012 Cited by PubMed Abstract: In bacteria, the hybrid transfer-messenger RNA (tmRNA) rescues ribosomes stalled on defective messenger RNAs (mRNAs). However, certain gram-negative bacteria have evolved proteins that are capable of rescuing stalled ribosomes in a tmRNA-independent manner. Here, we report a 3.2 angstrom-resolution crystal structure of the rescue factor YaeJ bound to the Thermus thermophilus 70S ribosome in complex with the initiator tRNA(i)(fMet) and a short mRNA. The structure reveals that the C-terminal tail of YaeJ functions as a sensor to discriminate between stalled and actively translating ribosomes by binding in the mRNA entry channel downstream of the A site between the head and shoulder of the 30S subunit. This allows the N-terminal globular domain to sample different conformations, so that its conserved GGQ motif is optimally positioned to catalyze the hydrolysis of peptidyl-tRNA. This structure gives insights into the mechanism of YaeJ function and provides a basis for understanding how it rescues stalled ribosomes. PubMed: 22422986DOI: 10.1126/science.1217443 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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