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Title | Molecular architecture of the HerA-NurA DNA double-strand break resection complex. |
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Journal, issue, pages | FEBS Lett, Vol. 588, Issue 24, Page 4637-4644, Year 2014 |
Publish date | Dec 20, 2014 |
![]() | Robert Thomas Byrne / Jan Michael Schuller / Pia Unverdorben / Friedrich Förster / Karl-Peter Hopfner / ![]() |
PubMed Abstract | DNA double-strand breaks can be repaired by homologous recombination, during which the DNA ends are long-range resected by helicase-nuclease systems to generate 3' single strand tails. In archaea, ...DNA double-strand breaks can be repaired by homologous recombination, during which the DNA ends are long-range resected by helicase-nuclease systems to generate 3' single strand tails. In archaea, this requires the Mre11-Rad50 complex and the ATP-dependent helicase-nuclease complex HerA-NurA. We report the cryo-EM structure of Sulfolobus solfataricus HerA-NurA at 7.4Å resolution and present the pseudo-atomic model of the complex. HerA forms an ASCE hexamer that tightly interacts with a NurA dimer, with each NurA protomer binding three adjacent HerA HAS domains. Entry to NurA's nuclease active sites requires dsDNA to pass through a 23Å wide channel in the HerA hexamer. The structure suggests that HerA is a dsDNA translocase that feeds DNA into the NurA nuclease sites. |
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Methods | EM (single particle) |
Resolution | 7.35 Å |
Structure data | ![]() EMDB-2808: |
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