Design of a colicin E7 based chimeric zinc-finger nuclease

Eszter Németh, Gabriella K. Schilli, Gábor Nagy, Christoph Hasenhindl, Béla Gyurcsik, Chris Oostenbrink

Research output: Contribution to journalArticle

10 Citations (Scopus)


Colicin E7 is a natural bacterial toxin. Its nuclease domain (NColE7) enters the target cell and kills it by digesting the nucleic acids. The HNH-motif as the catalytic centre of NColE7 at the C-terminus requires the positively charged N-terminal loop for the nuclease activity - offering opportunities for allosteric control in a NColE7-based artificial nuclease. Accordingly, four novel zinc finger nucleases were designed by computational methods exploiting the special structural features of NColE7. The constructed models were subjected to MD simulations. The comparison of structural stability and functional aspects showed that these models may function as safely controlled artificial nucleases. This study was complemented by random mutagenesis experiments identifying potentially important residues for NColE7 function outside the catalytic region.

Original languageEnglish
Pages (from-to)841-850
Number of pages10
JournalJournal of Computer-Aided Molecular Design
Issue number8
Publication statusPublished - Aug 2014



  • Colicin E7
  • Computational protein design
  • Metalloenzyme
  • Zinc finger nuclease

ASJC Scopus subject areas

  • Drug Discovery
  • Computer Science Applications
  • Physical and Theoretical Chemistry

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