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2KC9

Structure of E. coli toxin RelE (R81A/R83A) mutant in the free state

Summary for 2KC9
Entry DOI10.2210/pdb2kc9/pdb
Related2KC8
NMR InformationBMRB: 16066
DescriptorToxin relE (1 entity in total)
Functional Keywordsrele, toxin, repressor, stress response, transcription, transcription regulation
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight11356.29
Authors
Li, G.,Zhang, Y.,Inouye, M.,Ikura, M. (deposition date: 2008-12-17, release date: 2009-03-17, Last modification date: 2024-05-22)
Primary citationLi, G.Y.,Zhang, Y.,Inouye, M.,Ikura, M.
Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site.
J.Biol.Chem., 284:14628-14636, 2009
Cited by
PubMed Abstract: In Escherichia coli, RelE toxin participates in growth arrest and cell death by inducing mRNA degradation at the ribosomal A-site under stress conditions. The NMR structures of a mutant of E. coli RelE toxin, RelE(R81A/R83A), with reduced toxicity and its complex with an inhibitory peptide from RelB antitoxin, RelB(C) (Lys(47)-Leu(79)), have been determined. In the free RelE(R81A/R83A) structure, helix alpha4 at the C terminus adopts a closed conformation contacting with the beta-sheet core and adjacent loops. In the RelE(R81A/R83A)-RelB(C) complex, helix alpha3(*) of RelB(C) displaces alpha4 of RelE(R81A/R83A) from the binding site on the beta-sheet core. This helix replacement results in neutralization of a conserved positively charged cluster of RelE by acidic residues from alpha3(*) of RelB. The released helix alpha4 becomes unfolded, adopting an open conformation with increased mobility. The displacement of alpha4 disrupts the geometry of critical residues, including Arg(81) and Tyr(87), in a putative active site of RelE toxin. Our structures indicate that RelB counteracts the toxic activity of RelE by displacing alpha4 helix from the catalytically competent position found in the free RelE structure.
PubMed: 19297318
DOI: 10.1074/jbc.M809656200
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2025-07-16公开中

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