Cryo-EM structure of uropathogenic Escherichia coli CysK:CdiA:tRNA complex
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ABSTRACT:
SUBMITTER: Kozo Tomita
PROVIDER: EMPIAR-12146 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Mechanism of activation of contact-dependent growth inhibition tRNase toxin by the amino acid biogenesis factor CysK in the bacterial competition system.
Feng Zhaohang Z Yashiro Yuka Y Tomita Kozo K
Nucleic acids research 20240904
Contact-dependent growth inhibition (CDI) is a bacterial competition mechanism, wherein the C-terminal toxin domain of CdiA protein (CdiA-CT) is transferred from one bacterium to another, impeding the growth of the toxin recipient. In uropathogenic Escherichia coli 536, CdiA-CT (CdiA-CTEC536) is a tRNA anticodon endonuclease that requires a cysteine biogenesis factor, CysK, for its activity. However, the mechanism underlying tRNA recognition and cleavage by CdiA-CTEC536 remains unresolved. Here, ...[more]
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