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Assembly and stability of Salmonella enterica ser. Typhi TolC protein in POPE and DMPE.
[typhoid]
In
this
work
we
assessed
the
suitability
of
two
different
lipid
membranes
for
the
simulation
of
a
TolC
protein
from
Salmonella
enterica
serovar
Typhi
.
The
TolC
protein
family
is
found
in
many
pathogenic
Gram
-negative
bacteria
including
Vibrio
cholera
and
Pseudomonas
aeruginosa
and
acts
as
an
outer
membrane
channel
for
expulsion
of
drug
and
toxin
from
the
cell
.
In
S
.
typhi
,
the
causative
agent
for
typhoid
fever
,
the
TolC
outer
membrane
protein
is
an
antigen
for
the
pathogen
.
The
lipid
environment
is
an
important
modulator
of
membrane
protein
structure
and
function
.
We
evaluated
the
conformation
of
the
TolC
protein
in
the
presence
of
DMPE
and
POPE
bilayers
using
molecular
dynamics
simulation
.
The
S
.
typhi
TolC
protein
exhibited
similar
conformational
dynamics
to
TolC
and
its
homologues
.
Conformational
flexibility
of
the
protein
is
seen
in
the
C-
terminal
,
extracellular
loops
,
and
α-helical
region
.
Despite
differences
in
the
two
lipids
,
significant
similarities
in
the
motion
of
the
protein
in
POPE
and
DMPE
were
observed
,
including
the
rotational
motion
of
the
C-
terminal
residues
and
the
partially
open
extracellular
loops
.
However
,
analysis
of
the
trajectories
demonstrated
effects
of
hydrophobic
matching
of
the
TolC
protein
in
the
membrane
,
particularly
in
the
lengthening
of
the
lipids
and
subtle
movements
of
the
protein
's
β-barrel
towards
the
lower
leaflet
in
DMPE
.
The
study
exhibited
the
use
of
molecular
dynamics
simulation
in
revealing
the
differential
effect
of
membrane
proteins
and
lipids
on
each
other
.
In
this
study
,
POPE
is
potentially
a
more
suitable
model
for
future
simulation
of
the
S
.
typhi
TolC
protein
.