Crystal structure of TcpK in complex with oriT DNA of the antibiotic resistance plasmid pCW3

Daouda A. K. Traore, Jessica A. Wisniewski, Sarena F. Flanigan, Paul J. Conroy, Santosh Panjikar, Yee-Foong Mok, Carmen Lao, Michael D. W. Griffin, Vicki Adams (), Julian I. Rood () and James C. Whisstock ()
Additional contact information
Daouda A. K. Traore: Monash University
Jessica A. Wisniewski: Monash University
Sarena F. Flanigan: Monash University
Paul J. Conroy: Monash University
Santosh Panjikar: Monash University
Yee-Foong Mok: University of Melbourne
Carmen Lao: Monash University
Michael D. W. Griffin: University of Melbourne
Vicki Adams: Monash University
Julian I. Rood: Monash University
James C. Whisstock: Monash University

Nature Communications, 2018, vol. 9, issue 1, 1-11

Abstract: Abstract Conjugation is fundamental for the acquisition of new genetic traits and the development of antibiotic resistance in pathogenic organisms. Here, we show that a hypothetical Clostridium perfringens protein, TcpK, which is encoded by the tetracycline resistance plasmid pCW3, is essential for efficient conjugative DNA transfer. Our studies reveal that TcpK is a member of the winged helix-turn-helix (wHTH) transcription factor superfamily and that it forms a dimer in solution. Furthermore, TcpK specifically binds to a nine-nucleotide sequence that is present as tandem repeats within the pCW3 origin of transfer (oriT). The X-ray crystal structure of the TcpK–TcpK box complex reveals a binding mode centered on and around the β-wing, which is different from what has been previously shown for other wHTH proteins. Structure-guided mutagenesis experiments validate the specific interaction between TcpK and the DNA molecule. Additional studies highlight that the TcpK dimer is important for specific DNA binding.

Date: 2018
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DOI: 10.1038/s41467-018-06096-2

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