標題: Multiple Pleomorphic Tetramers of Thermostable Direct Hemolysin from Grimontia hollisae in Exerting Hemolysis and Membrane Binding
作者: Wang, Yu-Kuo
Huang, Sheng-Cih
Chang, Chin-Yuan
Huang, Wan-Ting
Liao, Man-Jun
Yip, Bak-Sau
Chou, Feng-Pai
Li, Thomas Tien-Hsiung
Wu, Tung-Kung
交大名義發表
生物科技學系
National Chiao Tung University
Department of Biological Science and Technology
公開日期: 8-七月-2019
摘要: Oligomerization of protein into specific quaternary structures plays important biological functions, including regulation of gene expression, enzymes activity, and cell-cell interactions. Here, we report the determination of two crystal structures of the Grimontia hollisae (formally described as Vibrio hollisae) thermostable direct hemolysin (Gh-TDH), a pore-forming toxin. The toxin crystalized in the same space group of P2(1)2(1)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 similar to 50 angstrom 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.
URI: http://dx.doi.org/10.1038/s41598-019-46354-x
http://hdl.handle.net/11536/152259
ISSN: 2045-2322
DOI: 10.1038/s41598-019-46354-x
期刊: SCIENTIFIC REPORTS
Volume: 9
起始頁: 0
結束頁: 0
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