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Carr, Stephen, Penfold, Christopher N., Bamford, Vicki, James, Richard and Hemmings, Andrew M. 
ORCID: https://orcid.org/0000-0003-3053-3134
(2000)
The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9.
Structure, 8 (1).
pp. 57-66.
ISSN 0969-2126
Abstract
Background: E colicin proteins have three functional domains, each of which is implicated in one of the stages of killing Escherichia coli cells: receptor binding, translocation and cytotoxicity. The central (R) domain is responsible for receptor-binding activity whereas the N-terminal (T) domain mediates translocation, the process by which the C-terminal cytotoxic domain is transported from the receptor to the site of its cytotoxicity. The translocation of enzymatic E colicins like colicin E9 is dependent upon TolB but the details of the process are not known. Results: We have demonstrated a protein-protein interaction between the T domain of colicin E9 and TolB, an essential component of the tol-dependent translocation system in E. coli, using the yeast two-hybrid system. The crystal structure of TolB, a procaryotic tryptophan-aspartate (WD) repeat protein, reveals an N-terminal α+β domain based on a five-stranded mixed β sheet and a C-terminal six- bladed β-propeller domain. Conclusions: The results suggest that the TolB- box residues of the T domain of colicin E9 interact with the β-propeller domain of TolB. The protein-protein interactions of other β-propeller- containing proteins, the yeast yPrp4 protein and G proteins, are mediated by the loops or outer sheets of the propeller blades. The determination of the three-dimensional structure of the T domain-TolB complex and the isolation of mutations in TolB that abolish the interaction with the T domain will reveal fine details of the protein-protein interaction of TolB and the T domain of E colicins.
| Item Type: | Article |
|---|---|
| Additional Information: | Funding Information: We thank Jean Claude Lazzaroni for providing the tolB2 mutant. We also thank all members of our labs, past and present, for their hard work and enthusiastic support of the colicin project at UEA. We acknowledge access to the EMBL X31 and X11 beamlines at the DORIS storage ring, DESY, and to the SRS station 9.6, Daresbury Laboratory. The Colicin Research Group is generously supported by The Wellcome Trust and the Biotechnology and Biological Sciences Research Council of the UK. |
| Uncontrolled Keywords: | e colicins,protein-protein interaction,tolb,translocation,β propeller,structural biology,molecular biology ,/dk/atira/pure/subjectarea/asjc/1300/1315 |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 21 Jan 2025 01:04 |
| Last Modified: | 21 Jan 2025 01:04 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/98280 |
| DOI: | 10.1016/S0969-2126(00)00079-4 |
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