NDLI: The gating mechanism of the bacterial mechanosensitive channel MscL revealed by molecular dynamics simulations

Please wait, while we are loading the content...

The gating mechanism of the bacterial mechanosensitive channel MscL revealed by molecular dynamics simulations

Content Provider	PubMed Central
Author	Sawada, Yasuyuki Murase, Masaki Masahiro, Sokabe
Copyright Year	2012
Abstract	One of the ultimate goals of the study on mechanosensitive (MS) channels is to understand the biophysical mechanisms of how the MS channel protein senses forces and how the sensed force induces channel gating. The bacterial MS channel MscL is an ideal subject to reach this goal owing to its resolved 3D protein structure in the closed state on the atomic scale and large amounts of electrophysiological data on its gating kinetics. However, the structural basis of the dynamic process from the closed to open states in MscL is not fully understood. In this study, we performed molecular dynamics (MD) simulations on the initial process of MscL opening in response to a tension increase in the lipid bilayer. To identify the tension-sensing site(s) in the channel protein, we calculated interaction energy between membrane lipids and candidate amino acids (AAs) facing the lipids. We found that Phe78 has a conspicuous interaction with the lipids, suggesting that Phe78 is the primary tension sensor of MscL. Increased membrane tension by membrane stretch dragged radially the inner (TM1) and outer (TM2) helices of MscL at Phe78, and the force was transmitted to the pentagon-shaped gate that is formed by the crossing of the neighboring TM1 helices in the inner leaflet of the bilayer. The radial dragging force induced radial sliding of the crossing portions, leading to a gate expansion. Calculated energy for this expansion is comparable to an experimentally estimated energy difference between the closed and the first subconductance state, suggesting that our model simulates the initial step toward the full opening of MscL. The model also successfully mimicked the behaviors of a gain of function mutant (G22N) and a loss of function mutant (F78N), strongly supporting that our MD model did simulate some essential biophysical aspects of the mechano-gating in MscL.
Related Links	http://dx.doi.org/10.4161/chan.21895
Ending Page	331
Page Count	15
Starting Page	317
File Format	PDF
ISSN	19336950
e-ISSN	19336969
Journal	Channels
Issue Number	4
Volume Number	6
Language	English
Publisher	Landes Bioscience
Publisher Date	2012-07-01
Access Restriction	Open
Rights Holder	Landes Bioscience
Subject Keyword	Biophysics Biochemistry Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Medicine Biochemistry Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Molecular dynamics study on protein–water interplay in the mechanogating of the bacterial mechanosensitive channel MscL

Molecular dynamics study on protein–water interplay in the mechanogating of the bacterial mechanosensitive channel MscL

Investigating Lipid Composition Effects on the Mechanosensitive Channel of Large Conductance (MscL) Using Molecular Dynamics Simulations

Molecular dynamics study on protein–water interplay in the mechanogating of the bacterial mechanosensitive channel MscL

Structural determinants of MscL gating studied by molecular dynamics simulations.

Disulfide Trapping the Mechanosensitive Channel MscL into a Gating-Transition State

Gating of the Mechanosensitive Channel Protein MscL: The Interplay of Membrane and Protein

A novel force transduction pathway from a tension sensor to the gate in the mechano-gating of MscL channel

Electromechanical coupling model of gating the large mechanosensitive ion channel (MscL) of Escherichia coli by mechanical force.

The gating mechanism of the bacterial mechanosensitive channel MscL revealed by molecular dynamics simulations

Similar Documents

Molecular dynamics study on protein–water interplay in the mechanogating of the bacterial mechanosensitive channel MscL

Molecular dynamics study on protein–water interplay in the mechanogating of the bacterial mechanosensitive channel MscL

Investigating Lipid Composition Effects on the Mechanosensitive Channel of Large Conductance (MscL) Using Molecular Dynamics Simulations

Molecular dynamics study on protein–water interplay in the mechanogating of the bacterial mechanosensitive channel MscL

Structural determinants of MscL gating studied by molecular dynamics simulations.

Disulfide Trapping the Mechanosensitive Channel MscL into a Gating-Transition State

Gating of the Mechanosensitive Channel Protein MscL: The Interplay of Membrane and Protein

A novel force transduction pathway from a tension sensor to the gate in the mechano-gating of MscL channel

Electromechanical coupling model of gating the large mechanosensitive ion channel (MscL) of Escherichia coli by mechanical force.

The gating mechanism of the bacterial mechanosensitive channel MscL revealed by molecular dynamics simulations