Dynamic motion of bacterial surface pili based on structural analyses of covalently linked complexes formed by tip and shaft pili proteins from Clostridium perfringens.
The structures of complexes formed by covalently linking CppB and CppA by X-ray crystallography and cryo-EM analysis allowed us to construct a three-dimensional structure model with dynamic motion of C. perfringens pili, and proposed new insights into the mechanism by which CppB is preferentially attached to CppA.