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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Authors/Creators:
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:
  • Accepted: 29 November 2017
  • Published (online): 8 December 2017
  • Published: 16 February 2018
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: 06 Dec 2023 12:11
Published Version: https://doi.org/10.1093/nar/gkx1233
Status: Published
Refereed: Yes
Identification Number: https://doi.org/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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