Structural and functional examination of Neisseria gonorrhoeae TfpC reveals a dynamic two-domain architecture required for type IV pilus function

TfpC from Neisseria gonorrhoeae forms a dynamic three-stranded {beta}-sheet N-terminal domain linked to a C-terminal coiled-coil, and an acidic face is required for pilus biogenesis.

• Why it matters: Type IV pili are essential for Neisseria gonorrhoeae colonization and virulence, yet how TfpC’s domains build and operate the pilus machine was unclear.
• What they did: Using targeted structural and genetic approaches, the study mapped TfpC’s N-terminal domain as a dynamic three-stranded {beta}-sheet and tested functional requirements in the C-terminal coiled-coil, including an acidic face.
• The result: The flexible disordered region functions as a linker between N- and C-terminal domains, and TfpC’s acidic coiled-coil face is needed for full type IV pilus elaboration and function.

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