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 Transjournal_title
Biochemical Society transactionsauthors
Penfold CN,Li C,Zhang Y,Vankemmelbeke M,James Rdoi
10.1042/BST20120239subject
Has Abstractpub_date
2012-12-01 00:00:00pages
1469-74issue
6eissn
0300-5127issn
1470-8752pii
BST20120239journal_volume
40pub_type
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