6OXA

Dimeric E.coli YoeB bound to Thermus thermophilus 70S pre-cleavage (AAU)

This is a non-PDB format compatible entry.

Summary for 6OXA

• Entry DOI: 10.2210/pdb6oxa/pdb
• Descriptor: 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (59 entities in total)
• Functional Keywords: protein biosynthesis, ribosomes, rna, mrna, trna, transfer rna, 30s, 50s, 70s, 16s, 23s, ribosomal subunit, bacterial proteins, translation, bacterial translation, codon, decoding, frameshift suppressor, ribosome
• Biological source: Thermus thermophilus HB8; More
• Total number of polymer chains: 116
• Total formula weight: 4517856.69

Authors

Pavelich, I.J.,Hoffer, E.D.,Maehigashi, T.,Dunham, C.M. (deposition date: 2019-05-13, release date: 2019-08-21, Last modification date: 2024-10-30)

Primary citation

Pavelich, I.J.,Maehigashi, T.,Hoffer, E.D.,Ruangprasert, A.,Miles, S.J.,Dunham, C.M.
Monomeric YoeB toxin retains RNase activity but adopts an obligate dimeric form for thermal stability.
Nucleic Acids Res., 47:10400-10413, 2019

PubMed Abstract: Chromosomally-encoded toxin-antitoxin complexes are ubiquitous in bacteria and regulate growth through the release of the toxin component typically in a stress-dependent manner. Type II ribosome-dependent toxins adopt a RelE-family RNase fold and inhibit translation by degrading mRNAs while bound to the ribosome. Here, we present biochemical and structural studies of the Escherichia coli YoeB toxin interacting with both a UAA stop and an AAU sense codon in pre- and post-mRNA cleavage states to provide insights into possible mRNA substrate selection. Both mRNAs undergo minimal changes during the cleavage event in contrast to type II ribosome-dependent RelE toxin. Further, the 16S rRNA decoding site nucleotides that monitor the mRNA in the aminoacyl(A) site adopt different orientations depending upon which toxin is present. Although YoeB is a RelE family member, it is the sole ribosome-dependent toxin that is dimeric. We show that engineered monomeric YoeB is active against mRNAs bound to both the small and large subunit. However, the stability of monomeric YoeB is reduced ∼20°C, consistent with potential YoeB activation during heat shock in E. coli as previously demonstrated. These data provide a molecular basis for the ability of YoeB to function in response to thermal stress.

PubMed: 31501867
DOI: 10.1093/nar/gkz760

Experimental method

X-RAY DIFFRACTION (3.25 Å)