5VFX

Structure of an accessory protein of the pCW3 relaxosome in complex with the origin of transfer (oriT) DNA

5VFX の概要

• エントリーDOI: 10.2210/pdb5vfx/pdb
• 関連するPDBエントリー: 5VFY
• 分子名称: TcpK, oriT, ... (4 entities in total)
• 機能のキーワード: conjugation, winged helix-turn-helix, orit, clostridium perfringens, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Clostridium perfringens; 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 160513.05

構造登録者

Traore, D.A.K.,Wisniewski, J.A.,Flanigan, S.F.,Conroy, P.J.,Panjikar, S.,Mok, Y.-F.,Lao, C.,Griffin, M.D.W.,Adams, V.,Rood, J.I.,Whisstock, J.C. (登録日: 2017-04-10, 公開日: 2018-04-18, 最終更新日: 2023-10-04)

主引用文献

Traore, D.A.K.,Wisniewski, J.A.,Flanigan, S.F.,Conroy, P.J.,Panjikar, S.,Mok, Y.F.,Lao, C.,Griffin, M.D.W.,Adams, V.,Rood, J.I.,Whisstock, J.C.
Crystal structure of TcpK in complex with oriT DNA of the antibiotic resistance plasmid pCW3.
Nat Commun, 9:3732-3732, 2018

PubMed 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.

PubMed: 30213934
DOI: 10.1038/s41467-018-06096-2

実験手法

X-RAY DIFFRACTION (2.81 Å)