Design of a colicin E7 based chimeric zinc-finger nuclease
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- 作者：Eszter Németh (1)
Gabriella K. Schilli (1)
Gábor Nagy (2)
Christoph Hasenhindl (3)
Béla Gyurcsik (1) (4)
Chris Oostenbrink (2) - 关键词：Metalloenzyme ; Zinc finger nuclease ; Colicin E7 ; Computational protein design
- 刊名：Journal of Computer-Aided Molecular Design
- 出版年：2014
- 出版时间：August 2014
- 年：2014
- 卷：28
- 期：8
- 页码：841-850
- 全文大小：3,127 KB
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Gabriella K. Schilli (1)
Gábor Nagy (2)
Christoph Hasenhindl (3)
Béla Gyurcsik (1) (4)
Chris Oostenbrink (2)
1. Department of Inorganic and Analytical Chemistry, University of Szeged, Dóm tér 7, Szeged, 6720, Hungary
2. Institute of Molecular Modeling and Simulation, University of Natural Resources and Life Sciences (BOKU), Muthgasse 18, 1190, Vienna, Austria
3. Christian Doppler Laboratory for Antibody Engineering, Department of Chemistry, Vienna Institute of BioTechnology, University of Natural Resources and Life Sciences (BOKU), Muthgasse 18, 1190, Vienna, Austria
4. MTA-SzTE Bioinorganic Chemistry Research Group of Hungarian Academy of Sciences, Dóm tér 7, Szeged, 6720, Hungary - ISSN：1573-4951
文摘
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.