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Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin.

Kamada K, Hanaoka F
Mol Cell 19 497-509 (2005)
Related entries: 2a6r, 2a6s

Cited: 139 times
EuropePMC logo PMID: 16109374

Abstract

The eubacterial chromosome encodes various addiction modules that control global levels of translation through RNA degradation. Crystal structures of the Escherichia coli YefM2 (antitoxin)-YoeB (toxin) complex and the free YoeB toxin have been determined. The structure of the heterotrimeric complex reveals an asymmetric disorder-to-order recognition strategy, in which one C terminus of the YefM homodimer exclusively interacts with an atypical microbial ribonuclease (RNase) fold of YoeB. Comparison with the YefM-free YoeB structure indicates a conformational rearrangement of the RNase catalytic site of YoeB, induced by interaction with YefM. Complementary biochemical experiments demonstrate that the YoeB toxin has an in vitro RNase activity that preferentially cleaves at the 3' end of purine ribonucleotides.

Reviews - 2a6q mentioned but not cited (5)

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