Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects

Hisanori Takagi, Yoshimitsu Kakuta, Takahiro Okada, Min Yao, Isao Tanaka, Makoto Kimura

Research output: Contribution to journalArticlepeer-review

139 Citations (Scopus)

Abstract

The Escherichia coli chromosome encodes toxin-antitoxin pairs. The toxin RelE cleaves mRNA positioned at the A-site in ribosomes, whereas the antitoxin RelB relieves the effect of RelE. The hyperthermophilic archaeon Pyrococcus horikoshii OT3 has the archaeal homologs aRelE and aRelB. Here we report the crystal structure of aRelE in complex with aRelB determined at a resolution of 2.3 Å. aRelE folds into an α/β structure, whereas aRelB lacks a distinct hydrophobic core and extensively wraps around the molecular surface of aRelE. Neither component shows structural homology to known ribonucleases or their inhibitors. Site-directed mutagenesis suggests that Arg85, in the C-terminal region, is strongly involved in the functional activity of aRelE, whereas Arg40, Leu48, Arg58 and Arg65 play a modest role in the toxin's activity.

Original languageEnglish
Pages (from-to)327-331
Number of pages5
JournalNature Structural and Molecular Biology
Volume12
Issue number4
DOIs
Publication statusPublished - Dec 1 2005

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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