Colicin A binds to a novel binding site of TolA in the Escherichia coli periplasm.

Abstract:

: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.

journal_name

Biochem Soc Trans

authors

Penfold CN,Li C,Zhang Y,Vankemmelbeke M,James R

doi

10.1042/BST20120239

subject

Has Abstract

pub_date

2012-12-01 00:00:00

pages

1469-74

issue

6

eissn

0300-5127

issn

1470-8752

pii

BST20120239

journal_volume

40

pub_type

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