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.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Wang YK,Huang SC,Chang CY,Huang WT,Liao MJ,Yip BS,Chou FP,Li TT,Wu TKdoi
10.1038/s41598-019-46354-xsubject
Has Abstractpub_date
2019-07-08 00:00:00pages
9833issue
1issn
2045-2322pii
10.1038/s41598-019-46354-xjournal_volume
9pub_type
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