3A57

Crystal structure of Thermostable Direct Hemolysin

3A57 の概要

• エントリーDOI: 10.2210/pdb3a57/pdb
• 分子名称: Thermostable direct hemolysin 2 (2 entities in total)
• 機能のキーワード: hemolysin, cytolysis, disulfide bond, hemolysis, toxin
• 由来する生物種: Vibrio parahaemolyticus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18659.62

構造登録者

Hashimoto, H.,Yanagihara, I.,Nakahira, K.,Hamada, D.,Ikegami, T.,Mayanagi, K.,Kaieda, S.,Fukui, T.,Ohnishi, K.,Kajiyama, S.,Yamane, T.,Ikeguchi, M.,Honda, T.,Shimizu, T.,Sato, M. (登録日: 2009-08-03, 公開日: 2010-03-31, 最終更新日: 2024-10-16)

主引用文献

Yanagihara, I.,Nakahira, K.,Yamane, T.,Kaieda, S.,Mayanagi, K.,Hamada, D.,Fukui, T.,Ohnishi, K.,Kajiyama, S.,Shimizu, T.,Sato, M.,Ikegami, T.,Ikeguchi, M.,Honda, T.,Hashimoto, H.
Structure and functional characterization of Vibrio parahaemolyticus thermostable direct hemolysin
J.Biol.Chem., 285:16267-16274, 2010

PubMed Abstract: Thermostable direct hemolysin (TDH) is a major virulence factor of Vibrio parahaemolyticus that causes pandemic foodborne enterocolitis mediated by seafood. TDH exists as a tetramer in solution, and it possesses extreme hemolytic activity. Here, we present the crystal structure of the TDH tetramer at 1.5 A resolution. The TDH tetramer forms a central pore with dimensions of 23 A in diameter and approximately 50 A in depth. Pi-cation interactions between protomers comprising the tetramer were indispensable for hemolytic activity of TDH. The N-terminal region was intrinsically disordered outside of the pore. Molecular dynamic simulations suggested that water molecules permeate freely through the central and side channel pores. Electron micrographs showed that tetrameric TDH attached to liposomes, and some of the tetramer associated with liposome via one protomer. These findings imply a novel membrane attachment mechanism by a soluble tetrameric pore-forming toxin.

PubMed: 20335168
DOI: 10.1074/jbc.M109.074526

実験手法

X-RAY DIFFRACTION (1.5 Å)