Conformational dynamics and membrane interactions of the E. coli outer membrane protein FecA: A molecular dynamics simulation study

The TonB-dependent transporters mediate high-affinity binding and active transport of a variety of substrates across the outer membrane of Escherichia coli. The substrates transported by these proteins are large, scarce nutrients that are unable to gain entry into the cell by passive diffusion acros...

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Bibliographic Details
Main Authors: Piggot, Thomas J. (Author), Holdbrook, Daniel A. (Author), Khalid, Syma (Author)
Format: Article
Language:English
Published: 2013-02.
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Online Access:Get fulltext
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100 1 0 |a Piggot, Thomas J.  |e author 
700 1 0 |a Holdbrook, Daniel A.  |e author 
700 1 0 |a Khalid, Syma  |e author 
245 0 0 |a Conformational dynamics and membrane interactions of the E. coli outer membrane protein FecA: A molecular dynamics simulation study 
260 |c 2013-02. 
856 |z Get fulltext  |u https://eprints.soton.ac.uk/356327/1/Tom_paper_FecA.pdf 
520 |a The TonB-dependent transporters mediate high-affinity binding and active transport of a variety of substrates across the outer membrane of Escherichia coli. The substrates transported by these proteins are large, scarce nutrients that are unable to gain entry into the cell by passive diffusion across the complex, asymmetric bilayer that constitutes the outer membrane. Experimental studies have identified loop regions that are essential for the correct functioning of these proteins. A number of these loops have been implicated in ligand binding. We report the first simulations of an E. coli outer membrane protein in an asymmetric model membrane that incorporates lipopolysaccharide (LPS) molecules. Comparative simulations of the apo and holo forms of the TonB-dependent transporter FecA in different membrane models enable us to identify the nature of the LPS-protein interactions and determine how these interactions impact upon the conformational dynamics of this protein. In particular, our simulations provide molecular-level insights into the influence of the environment and ligand on the dynamics of the functionally important loops of FecA. In addition, we provide insights into the nature of the protein-ligand interactions and ligand induced conformational change in FecA. 
655 7 |a Article