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-Structure paper
Title | Mechanism for nuclease regulation in RecBCD. |
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Journal, issue, pages | Elife, Vol. 5, Year 2016 |
Publish date | Sep 20, 2016 |
Authors | Martin Wilkinson / Yuriy Chaban / Dale B Wigley / |
PubMed Abstract | In bacterial cells, processing of double-stranded DNA breaks for repair by homologous recombination is catalysed by AddAB, AdnAB or RecBCD-type helicase-nucleases. These enzyme complexes are highly ...In bacterial cells, processing of double-stranded DNA breaks for repair by homologous recombination is catalysed by AddAB, AdnAB or RecBCD-type helicase-nucleases. These enzyme complexes are highly processive, duplex unwinding and degrading machines that require tight regulation. Here, we report the structure of E.coli RecBCD, determined by cryoEM at 3.8 Å resolution, with a DNA substrate that reveals how the nuclease activity of the complex is activated once unwinding progresses. Extension of the 5'-tail of the unwound duplex induces a large conformational change in the RecD subunit, that is transferred through the RecC subunit to activate the nuclease domain of the RecB subunit. The process involves a SH3 domain that binds to a region of the RecB subunit in a binding mode that is distinct from others observed previously in SH3 domains and, to our knowledge, this is the first example of peptide-binding of an SH3 domain in a bacterial system. |
External links | Elife / PubMed:27644322 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.83 Å |
Structure data | |
Chemicals | ChemComp-ANP: ChemComp-MG: |
Source |
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Keywords | HYDROLASE / Helicase / Nuclease / SH3 / Homologous Recombination |