Maltose binding protein (MalE) interacts with periplasmic loops P2 and P1 respectively of the MalFG subunits of the maltose ATP binding cassette transporter (MalFGK2) from Escherichia coli/Salmonella during the transport cycle-Reference-Cited by-同舟云学术

Maltose binding protein (MalE) interacts with periplasmic loops P2 and P1 respectively of the MalFG subunits of the maltose ATP binding cassette transporter (MalFGK2) from Escherichia coli/Salmonella during the transport cycle

Published:2007-12 Issue:5 Volume:66 Page:1107-1122
ISSN:0950-382X
Container-title:Molecular Microbiology
language:en
Short-container-title:Mol Microbiol

Author:

Daus Martin L.,Berendt Susanne,Wuttge Steven,Schneider Erwin

Publisher

Wiley

Subject

Molecular Biology,Microbiology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2958.2007.05982.x/fullpdf

Reference55 articles.

1. Liganded and Unliganded Receptors Interact with Equal Affinity with the Membrane Complex of Periplasmic Permeases, a Subfamily of Traffic ATPases

2. The requirement for energy during export of beta-lactamase in Escherichia coli is fulfilled by the total protonmotive force.

3. On the role of the two extracytoplasmic substrate-binding domains in the ABC transporter OpuA

4. Mathematical treatment of the kinetics of binding protein dependent transport systems reveals that both the substrate loaded and unloaded binding proteins interact with the membrane components

5. Maltose/Maltodextrin System of Escherichia coli : Transport, Metabolism, and Regulation

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