Fig. 1: TssA proteins form ring structures with peripheral conserved Nt1 domains. | Nature Communications

Fig. 1: TssA proteins form ring structures with peripheral conserved Nt1 domains.

From: Functionality of chimeric TssA proteins in the type VI secretion system reveals sheath docking specificity within their N-terminal domains

Fig. 1

a In TssAS proteins, such as P. aeruginosa TssA1 and TssA3, a flexible linker (grey) connects the Nt1 domain (yellow) to the C-terminal domain (CTD) (red). Oligomerisation of the TssAS CTD forms a ring-shaped structure with peripheral Nt1 domains. b In TssAL proteins, such as P. aeruginosa TssA2, a flexible linker connects the Nt1 domain to the Nt2 domain (purple). The Nt2 domain is then connected by a flexible linker to a distinct TssAL CTD (blue). Oligomerisation of the TssAL CTD forms a ring-shaped structure with peripheral Nt2 domain dimers connecting to Nt1 domains.

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