4V7K
Structure of RelE nuclease bound to the 70S ribosome (postcleavage state)
This is a non-PDB format compatible entry.
Summary for 4V7K
| Entry DOI | 10.2210/pdb4v7k/pdb |
| Related | 3KIQ 3KIR 3KIS 3KIT |
| Descriptor | 30S ribosomal protein S2, 30S ribosomal protein S11, 30S ribosomal protein S12, ... (60 entities in total) |
| Functional Keywords | ribosome, translational control, relbe, toxin-antitoxin, endonuclease, coiled coil, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, metal-binding, zinc, zinc-finger, trna-binding, repressor, stress response, toxin, translation, translation regulation |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 116 |
| Total formula weight | 4525503.15 |
| 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: 2024-11-06) |
| 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 Cited by 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: 20005802DOI: 10.1016/j.cell.2009.11.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.6 Å) |
Structure validation
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