To gate or not to gate: using molecular dynamics simulations to morph gated plant aquaporins into constitutively open conformations

Himanshu Khandelia; Morten O. Jensen; Ole G. Mouritsen

doi:10.1021/jp809152c

To gate or not to gate: using molecular dynamics simulations to morph gated plant aquaporins into constitutively open conformations

Himanshu Khandelia^*, Morten O. Jensen, Ole G. Mouritsen

^*Corresponding author for this work

21 Citations (Scopus)

Abstract

The spinach plant aquaporin SoPIP2;1 is a gated water channel, which switches between open and closed states depending on the conformation of a 20-residue cytoplasmic loop, the D-loop. Using fully atomistic molecular dynamics simulations, we have investigated the possibility of driving the conformational equilibrium of the protein toward a constitutively open state. We introduce two separate mutations in the D-loop, while being in the closed conformation. We show that the single channel permeability of both mutants is comparable to that of the open conformation. This Article provides new molecular insight into the gating mechanism of SoPIP2;1. It is proposed that residues Arg190, Asp191, and Ser36 might play important roles in the gating of the protein.

Original language	English
Journal	Journal of Physical Chemistry B
Volume	113
Issue number	15
Pages (from-to)	5239-5244
Number of pages	6
ISSN	1520-6106
DOIs	https://doi.org/10.1021/jp809152c
Publication status	Published - 16 Apr 2009

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abstract = "The spinach plant aquaporin SoPIP2;1 is a gated water channel, which switches between open and closed states depending on the conformation of a 20-residue cytoplasmic loop, the D-loop. Using fully atomistic molecular dynamics simulations, we have investigated the possibility of driving the conformational equilibrium of the protein toward a constitutively open state. We introduce two separate mutations in the D-loop, while being in the closed conformation. We show that the single channel permeability of both mutants is comparable to that of the open conformation. This Article provides new molecular insight into the gating mechanism of SoPIP2;1. It is proposed that residues Arg190, Asp191, and Ser36 might play important roles in the gating of the protein.",

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T1 - To gate or not to gate

T2 - using molecular dynamics simulations to morph gated plant aquaporins into constitutively open conformations

AU - Khandelia, Himanshu

AU - Jensen, Morten O.

AU - Mouritsen, Ole G.

PY - 2009/4/16

Y1 - 2009/4/16

N2 - The spinach plant aquaporin SoPIP2;1 is a gated water channel, which switches between open and closed states depending on the conformation of a 20-residue cytoplasmic loop, the D-loop. Using fully atomistic molecular dynamics simulations, we have investigated the possibility of driving the conformational equilibrium of the protein toward a constitutively open state. We introduce two separate mutations in the D-loop, while being in the closed conformation. We show that the single channel permeability of both mutants is comparable to that of the open conformation. This Article provides new molecular insight into the gating mechanism of SoPIP2;1. It is proposed that residues Arg190, Asp191, and Ser36 might play important roles in the gating of the protein.

AB - The spinach plant aquaporin SoPIP2;1 is a gated water channel, which switches between open and closed states depending on the conformation of a 20-residue cytoplasmic loop, the D-loop. Using fully atomistic molecular dynamics simulations, we have investigated the possibility of driving the conformational equilibrium of the protein toward a constitutively open state. We introduce two separate mutations in the D-loop, while being in the closed conformation. We show that the single channel permeability of both mutants is comparable to that of the open conformation. This Article provides new molecular insight into the gating mechanism of SoPIP2;1. It is proposed that residues Arg190, Asp191, and Ser36 might play important roles in the gating of the protein.

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SN - 1520-6106

VL - 113

SP - 5239

EP - 5244

JO - Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical

JF - Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical

IS - 15

ER -

To gate or not to gate: using molecular dynamics simulations to morph gated plant aquaporins into constitutively open conformations

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