Recombination directionality factor gp3 binds ϕC31 integrase via the zinc domain, potentially affecting the trajectory of the coiled-coil motif

Fogg, Paul C M orcid.org/0000-0001-5324-4293, Younger, Ellen, Fernando, Booshini D et al. (3 more authors) (2018) Recombination directionality factor gp3 binds ϕC31 integrase via the zinc domain, potentially affecting the trajectory of the coiled-coil motif. Nucleic Acids Research. pp. 1308-1320. ISSN 0305-1048

Abstract

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Item Type: Article
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Copyright, Publisher and Additional Information:

© The Author(s) 2017.

Keywords: Journal Article,Attachment Sites, Microbiological,Lysogeny,Integrases/chemistry,Recombinant Proteins/chemistry,Thermodynamics,Viral Proteins/chemistry,Cloning, Molecular,Protein Interaction Domains and Motifs,DNA, Bacterial/chemistry,Binding Sites,Genetic Vectors/chemistry,Streptomyces/chemistry,Amino Acid Sequence,Protein Conformation, alpha-Helical,Gene Expression,Models, Molecular,DNA-Binding Proteins/chemistry,Escherichia coli/genetics,Sequence Homology, Amino Acid,Sequence Alignment,Protein Conformation, beta-Strand,Siphoviridae/chemistry,Protein Binding,Mutation,Amino Acid Substitution
Dates:
  • Published: 16 February 2018
  • Published (online): 8 December 2017
  • Accepted: 29 November 2017
Institution: The University of York
Academic Units: The University of York > Faculty of Sciences (York) > Biology (York)
Depositing User: Pure (York)
Date Deposited: 20 Dec 2017 09:10
Last Modified: 21 Jan 2025 17:29
Published Version: https://doi.org/10.1093/nar/gkx1233
Status: Published
Refereed: Yes
Identification Number: 10.1093/nar/gkx1233
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Description: Recombination directionality factor gp3 binds C31 integrase via the zinc domain, potentially affecting the trajectory of the coiled-coil motif

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