4V7J

Structure of RelE nuclease bound to the 70S ribosome (precleavage state)

This is a non-PDB format compatible entry.

Summary for 4V7J

• Entry DOI: 10.2210/pdb4v7j/pdb
• Related: 3KIU 3KIW 3KIX 3KIY
• Descriptor: 30S ribosomal protein S2, 30S ribosomal protein S11, 30S ribosomal protein S12, ... (60 entities in total)
• Functional Keywords: ribosome, rele, nuclease, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, metal-binding, zinc-finger, trna-binding, antibiotic resistance, repressor, stress response, toxin, translation, translation regulation
• Biological source: Escherichia coli K-12; More
• Total number of polymer chains: 116
• Total formula weight: 4532553.44

Authors

Neubauer, C.,Gao, Y.-G.,Andersen, K.R.,Dunham, C.M.,Kelley, A.C.,Hentschel, J.,Gerdes, K.,Ramakrishnan, V.,Brodersen, D.E. (deposition date: 2009-11-02, release date: 2014-07-09, Last modification date: 2024-10-16)

Primary citation

Neubauer, C.,Gao, Y.G.,Andersen, K.R.,Dunham, C.M.,Kelley, A.C.,Hentschel, J.,Gerdes, K.,Ramakrishnan, V.,Brodersen, D.E.
The structural basis for mRNA recognition and cleavage by the ribosome-dependent endonuclease RelE.
Cell(Cambridge,Mass.), 139:1084-1095, 2009

PubMed Abstract: Translational control is widely used to adjust gene expression levels. During the stringent response in bacteria, mRNA is degraded on the ribosome by the ribosome-dependent endonuclease, RelE. The molecular basis for recognition of the ribosome and mRNA by RelE and the mechanism of cleavage are unknown. Here, we present crystal structures of E. coli RelE in isolation (2.5 A) and bound to programmed Thermus thermophilus 70S ribosomes before (3.3 A) and after (3.6 A) cleavage. RelE occupies the A site and causes cleavage of mRNA after the second nucleotide of the codon by reorienting and activating the mRNA for 2'-OH-induced hydrolysis. Stacking of A site codon bases with conserved residues in RelE and 16S rRNA explains the requirement for the ribosome in catalysis and the subtle sequence specificity of the reaction. These structures provide detailed insight into the translational regulation on the bacterial ribosome by mRNA cleavage.

PubMed: 20005802
DOI: 10.1016/j.cell.2009.11.015

Experimental method

X-RAY DIFFRACTION (3.3 Å)