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TitleA conformational switch in response to Chi converts RecBCD from phage destruction to DNA repair.
Journal, issue, pagesNat Struct Mol Biol, Vol. 27, Issue 1, Page 71-77, Year 2020
Publish dateJan 6, 2020
AuthorsKaiying Cheng / Martin Wilkinson / Yuriy Chaban / Dale B Wigley /
PubMed AbstractThe RecBCD complex plays key roles in phage DNA degradation, CRISPR array acquisition (adaptation) and host DNA repair. The switch between these roles is regulated by a DNA sequence called Chi. We ...The RecBCD complex plays key roles in phage DNA degradation, CRISPR array acquisition (adaptation) and host DNA repair. The switch between these roles is regulated by a DNA sequence called Chi. We report cryo-EM structures of the Escherichia coli RecBCD complex bound to several different DNA forks containing a Chi sequence, including one in which Chi is recognized and others in which it is not. The Chi-recognized structure shows conformational changes in regions of the protein that contact Chi and reveals a tortuous path taken by the DNA. Sequence specificity arises from interactions with both the RecC subunit and the sequence itself. These structures provide molecular details for how Chi is recognized and insights into the changes that occur in response to Chi binding that switch RecBCD from bacteriophage destruction and CRISPR spacer acquisition to constructive host DNA repair.
External linksNat Struct Mol Biol / PubMed:31907455 / PubMed Central
MethodsEM (single particle)
Resolution3.6 - 4.1 Å
Structure data

10214

6sjb

EMDB-10214, PDB-6sjb:
Cryo-EM structure of the RecBCD Chi recognised complex
Method: EM (single particle) / Resolution: 3.7 Å

10215

6sje

EMDB-10215, PDB-6sje:
Cryo-EM structure of the RecBCD Chi partially-recognised complex
Method: EM (single particle) / Resolution: 4.1 Å

10216

6sjf

EMDB-10216, PDB-6sjf:
Cryo-EM structure of the RecBCD Chi unrecognised complex
Method: EM (single particle) / Resolution: 3.9 Å

10217

6sjg

EMDB-10217, PDB-6sjg:
Cryo-EM structure of the RecBCD no Chi negative control complex
Method: EM (single particle) / Resolution: 3.8 Å

10369

6t2u

EMDB-10369, PDB-6t2u:
Cryo-EM structure of the RecBCD in complex with Chi-minus2 substrate
Method: EM (single particle) / Resolution: 3.6 Å

10370

6t2v

EMDB-10370, PDB-6t2v:
Cryo-EM structure of the RecBCD in complex with Chi-plus2 substrate
Method: EM (single particle) / Resolution: 3.8 Å

Source
  • escherichia coli (E. coli)
  • synthetic construct (others)
KeywordsHYDROLASE / DNA repair / Homologous recombination / ATP hydrolysis / Helicase / Nuclease / translocation

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