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Title
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Understanding Voltage Gating of Providencia stuartii Porins at Atomic Level.
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Authors
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W.Song,
H.Bajaj,
C.Nasrallah,
H.Jiang,
M.Winterhalter,
J.P.Colletier,
Y.Xu.
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Ref.
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PLoS Comput Biol, 2015,
11,
e1004255.
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PubMed id
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Abstract
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Bacterial porins are water-filled β-barrel channels that allow translocation of
solutes across the outer membrane. They feature a constriction zone, contributed
by the plunging of extracellular loop 3 (L3) into the channel lumen. Porins are
generally in the open state, but undergo gating in response to external
voltages. To date the underlying mechanism is unclear. Here we report results
from molecular dynamics simulations on the two porins of Providenica stuartii,
Omp-Pst1 and Omp-Pst2, which display distinct voltage sensitivities. Voltage
gating was observed in Omp-Pst2, where the binding of cations in-between L3 and
the barrel wall results in exposing a conserved aromatic residue in the channel
lumen, thereby halting ion permeation. Comparison of Omp-Pst1 and Omp-Pst2
structures and trajectories suggests that their sensitivity to voltage is
encoded in the hydrogen-bonding network anchoring L3 onto the barrel wall, as we
observed that it is the strength of this network that governs the probability of
cations binding behind L3. That Omp-Pst2 gating is observed only when ions flow
against the electrostatic potential gradient of the channel furthermore suggests
a possible role for this porin in the regulation of charge distribution across
the outer membrane and bacterial homeostasis.
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