Dimerization of the type IV pilin from Pseudomonas aeruginosa strain K122-4 results in increased helix stability as measured by time-resolved hydrogen-deuterium exchange

Structural Dynamics
Cristina LentoGerald F Audette

Abstract

Truncated pilin monomers from Pseudomonas aeruginosa strain K122-4 (ΔK122) have been shown to enter a monomer-dimer equilibrium in solution prior to oligomerization into protein nanotubes. Here, we examine the structural changes occurring between the monomeric and dimeric states of ΔK122 using time-resolved hydrogen-deuterium exchange mass spectrometry. Based on levels of deuterium uptake, the N-terminal α-helix and the loop connecting the second and third strands of the anti-parallel β-sheet contribute significantly to pilin dimerization. Conversely, the antiparallel β-sheet and αβ loop region exhibit increased flexibility, while the receptor binding domain retains a rigid conformation in the equilibrium state.

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Citations

Apr 5, 2016·Structural Dynamics·George N Phillips, José N Onuchic
Apr 21, 2017·Dalton Transactions : an International Journal of Inorganic Chemistry·Yuanyuan WangFuyi Wang
Jun 27, 2019·Biomedicines·Gerald F AudetteRaj Bawa
Sep 24, 2020·Biomedicines·Nicholas BragagnoloGerald F Audette

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Methods Mentioned

BETA
chip
electrophoresis
NMR

Software Mentioned

TRESI
FindPept
HDX
ExPASy
FORTRAN
CorelDraw X3
Sigma Plot

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