Multiple Pleomorphic Tetramers of Thermostable Direct Hemolysin from Grimontia hollisae in Exerting Hemolysis and Membrane Binding

Yu Kuo Wang, Sheng Cih Huang, Chin-Yuan Chang, Wan Ting Huang, Man Jun Liao, Bak Sau Yip, Feng Pai Chou, Thomas Tien Hsiung Li, Tung-Kung Wu*

*Corresponding author for this work

Research output: Contribution to journalArticle

Abstract

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 P21212, 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.

Original languageEnglish
Article number9833
JournalScientific reports
Volume9
Issue number1
DOIs
StatePublished - 8 Jul 2019

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