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microtubule formation mechanism structural and functional analysis of HSP90 bacteriophage tubulins advanced microscopies
In collaboration with Joe Pogliano (UCSD) we have discovered a family of tubulins encoded by very large bacteriophage (~300Kb), and have determined the crystal structure of the first phage cytoskeletal element - a tubulin family member known as PhuZ. While longitudinal interactions are well conserved in all tubulins, the crystal structure which mimics longitudinal packing in the filaments, revealed a gap between molecules. Instead, filaments are formed by a novel C-terminal extension that directly links molecules in the filament. In vivo observations of infected cells reveals that PhuZ forms a spindle like structure that position phage particles at the cell midline. Altering PhuZ dynamics leads to phage mis-positioning and a significantly decreased burst size. In a continued collaboration, we now focus on understanding the cell and structural biology underlying this remarkable observation.

Crystal Lattice Contains Filament-like Contacts with the C-Terminal Tail Providing Most of the Contact Surface. Shown is a zoomed-in view showing the electrostatic surface of PhuZ interacting with the C-terminal tail. The tail buries 1,226 Å2 of surface area per monomer.

"A phage tubulin assembles dynamic filaments by a novel mechanism to center viral DNA within the host cell," J. Kraemer, M.L. Erb, C.A. Waddling, E.A. Montabana, E.A. Zehr, H. Wang, K. Nguyen, D.S.L. Pham, D. Agard, and J. Pogliano, Cell, 2012, 149(7), 1488-99 (html, pdf).

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