Multiple Pleomorphic Tetramers of Thermostable Direct Hemolysin from Grimontia hollisae in Exerting Hemolysis and Membrane Binding
Journal
Scientific Reports
Journal Volume
9
Journal Issue
1
Pages
9833
Date Issued
2019
Author(s)
Wang, Yu-Kuo ; Huang, Sheng-Cih ; Chang, Chin-Yuan ; Huang, Wan-Ting ; Liao, Man-Jun ; Chou, Feng-Pai ; Li, Li, Thomas Tien-Hsiung ; Wu, Tung-Kung
Abstract
2, but with two different crystal packing patterns, each revealing three consistent tetrameric oligomerization forms called Oligomer-I, -II, and -III. A central pore with comparable depth of ~50 Å but differing in shape and size was observed in all determined toxin tetrameric oligomers. A common motif of a toxin dimer was found in all determined structures, suggesting a plausible minimum functional unit within the tetrameric structure in cell membrane binding and possible hemolytic activity. Our results show that bacterial toxins may form a single or highly symmetric oligomerization state when exerting their biological functions. The dynamic nature of multiple symmetric oligomers formed upon release of the toxin may open a niche for bacteria survival in harsh living environments.
Type
journal article