4LEL

Crystal Structure of Frameshift Suppressor tRNA SufA6 Bound to Codon CCG-G on the Ribosome

This is a non-PDB format compatible entry.

Summary for 4LEL

• Entry DOI: 10.2210/pdb4lel/pdb
• Descriptor: 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (59 entities in total)
• Functional Keywords: protein biosynthesis, ribosomes, rna, trna, transfer rna, 30s, 70s, 16s, 23s, ribosomal subunit, ribosome
• Biological source: Thermus thermophilus; More
• Total number of polymer chains: 112
• Total formula weight: 4435746.02

Authors

Maehigashi, T.,Dunkle, J.A.,Dunham, C.M. (deposition date: 2013-06-25, release date: 2014-08-06, Last modification date: 2023-09-20)

Primary citation

Maehigashi, T.,Dunkle, J.A.,Miles, S.J.,Dunham, C.M.
Structural insights into +1 frameshifting promoted by expanded or modification-deficient anticodon stem loops.
Proc.Natl.Acad.Sci.USA, 111:12740-12745, 2014

PubMed Abstract: Maintenance of the correct reading frame on the ribosome is essential for accurate protein synthesis. Here, we report structures of the 70S ribosome bound to frameshift suppressor tRNA(SufA6) and N1-methylguanosine at position 37 (m(1)G37) modification-deficient anticodon stem loop(Pro), both of which cause the ribosome to decode 4 rather than 3 nucleotides, resulting in a +1 reading frame. Our results reveal that decoding at +1 suppressible codons causes suppressor tRNA(SufA6) to undergo a rearrangement of its 5' stem that destabilizes U32, thereby disrupting the conserved U32-A38 base pair. Unexpectedly, the removal of the m(1)G37 modification of tRNA(Pro) also disrupts U32-A38 pairing in a structurally analogous manner. The lack of U32-A38 pairing provides a structural correlation between the transition from canonical translation and a +1 reading of the mRNA. Our structures clarify the molecular mechanism behind suppressor tRNA-induced +1 frameshifting and advance our understanding of the role played by the ribosome in maintaining the correct translational reading frame.

PubMed: 25128388
DOI: 10.1073/pnas.1409436111

Experimental method

X-RAY DIFFRACTION (3.90000024172 Å)