STRUCTURAL ANALYSIS FOR THE ASSEMBLY MACHINERY FOR TYPE IV PILUS AND ITS RELATED

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Type IV pili (T4P) are filamentous structures exposed on surface of Gram-negative bacteria. The T4P are key virulence factors for human bacterial pathogens including Pseudomonas aeruginosa, Neisseria gonorrhea, and Vibrio cholerae. T4P filament is composed of 10,000 of copies of a single subunit, which has a highly conserved N-terminal hydrophobic sequence, responsible for its assembly. This interesting feature is also seen in other subutnits in different bacterial systems; type II secretion and the archaeal flagellar system. Both systems also contain T4P like subunits to form filament. Furthermore, other proteins involved in the subunit assembly in these systems resemble with each other. Among them, we are focusing on an assembly ATPase family, which assemble pilin subunits utilizing ATP hydrolysis energy. We have been studying Type IV pilus subunit, and have solved the crystal structures of N. gonorrhea, P. aeruginosa, and V. cholerae pilin subunits. In this proposal, we will solve the structure of Dichelobactor nodosus pilin as different type of pilus, P. aeruginosa XcpT as filament subunit of type II secretion system, and afGspE2 as an assembly ATPase for archaeal flagellar.