3D8A

Co-crystal structure of TraM-TraD complex.

3D8A の概要

• エントリーDOI: 10.2210/pdb3d8a/pdb
• 関連するPDBエントリー: 2G7O
• 分子名称: Relaxosome protein TraM, Protein traD (3 entities in total)
• 機能のキーワード: tram tetramerization domain, trad c-terminal peptide, protein complex, conjugation, dna-binding, atp-binding, inner membrane, membrane, nucleotide-binding, transmembrane, dna binding protein
• 由来する生物種: Escherichia coli (strain K12); 詳細
• 細胞内の位置: Cytoplasm : P10026
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 72479.42

構造登録者

Glover, J.N.M.,Lu, J.,Wong, J.J.,Edwards, R.A. (登録日: 2008-05-22, 公開日: 2008-09-09, 最終更新日: 2023-08-30)

主引用文献

Lu, J.,Wong, J.J.,Edwards, R.A.,Manchak, J.,Frost, L.S.,Glover, J.N.
Structural basis of specific TraD-TraM recognition during F plasmid-mediated bacterial conjugation.
Mol.Microbiol., 70:89-99, 2008

PubMed Abstract: F plasmid-mediated bacterial conjugation requires interactions between a relaxosome component, TraM, and the coupling protein TraD, a hexameric ring ATPase that forms the cytoplasmic face of the conjugative pore. Here we present the crystal structure of the C-terminal tail of TraD bound to the TraM tetramerization domain, the first structural evidence of relaxosome-coupling protein interactions. The structure reveals the TraD C-terminal peptide bound to each of four symmetry-related grooves on the surface of the TraM tetramer. Extensive protein-protein interactions were observed between the two proteins. Mutational analysis indicates that these interactions are specific and required for efficient F conjugation in vivo. Our results suggest that specific interactions between the C-terminal tail of TraD and the TraM tetramerization domain might lead to more generalized interactions that stabilize the relaxosome-coupling protein complex in preparation for conjugative DNA transfer.

PubMed: 18717787
DOI: 10.1111/j.1365-2958.2008.06391.x

実験手法

X-RAY DIFFRACTION (2.55 Å)