Colicins are protein antibiotics produced by Escherichia coli to kill closely related non-identical competing species. They have taken advantage of the promiscuity of several proteins in the cell envelope for entry into the bacterial cell. The Tol–Pal system comprises one such ensemble of periplasmic and membrane-associated interacting proteins that links the IM (inner membrane) and OM (outer membrane) and provides the cell with a structural scaffold for cell division and energy transduction. Central to the Tol–Pal system is the TolA hub protein which forms protein–protein interactions with all other members and also with extrinsic proteins such as colicins A, E1, E2–E9 and N, and the coat proteins of the Ff family of filamentous bacteriophages. In the present paper, we review the role of TolA in the translocation of colicin A through the recently determined crystal structure of the complex of TolA with a translocation domain peptide of ColA (TA53–107), we demonstrate that TA53–107 binds to TolA at a novel binding site and compare the interactions of TolA with other colicins that use the Tol–Pal system for cell entry substantiating further the role of TolA as a periplasmic hub protein.
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Conference Article|
November 21 2012
Colicin A binds to a novel binding site of TolA in the Escherichia coli periplasm
Christopher N. Penfold;
Christopher N. Penfold
1
1School of Molecular Medical Sciences, Centre for Biomolecular Sciences, University of Nottingham, University Park, Nottingham NG7 2RD, U.K.
1To whom correspondence should be addressed (emailchris.penfold@nottingham.ac.uk).
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Chan Li;
Chan Li
1School of Molecular Medical Sciences, Centre for Biomolecular Sciences, University of Nottingham, University Park, Nottingham NG7 2RD, U.K.
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Ying Zhang;
Ying Zhang
1School of Molecular Medical Sciences, Centre for Biomolecular Sciences, University of Nottingham, University Park, Nottingham NG7 2RD, U.K.
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Mireille Vankemmelbeke;
Mireille Vankemmelbeke
1School of Molecular Medical Sciences, Centre for Biomolecular Sciences, University of Nottingham, University Park, Nottingham NG7 2RD, U.K.
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Richard James
Richard James
1School of Molecular Medical Sciences, Centre for Biomolecular Sciences, University of Nottingham, University Park, Nottingham NG7 2RD, U.K.
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Publisher: Portland Press Ltd
Received:
September 13 2012
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2012 The Authors Journal
2012
Biochem Soc Trans (2012) 40 (6): 1469–1474.
Article history
Received:
September 13 2012
Citation
Christopher N. Penfold, Chan Li, Ying Zhang, Mireille Vankemmelbeke, Richard James; Colicin A binds to a novel binding site of TolA in the Escherichia coli periplasm. Biochem Soc Trans 1 December 2012; 40 (6): 1469–1474. doi: https://doi.org/10.1042/BST20120239
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