PMID:10673426

Citation	Carr, S, Penfold, CN, Bamford, V, James, R and Hemmings, AM (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 8:57-66
Abstract	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.
Links	PubMed
Keywords	Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Binding Sites; Colicins/chemistry; Colicins/genetics; Colicins/metabolism; Crystallography, X-Ray; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Periplasmic Proteins; Protein Conformation; Protein Structure, Tertiary; Sequence Deletion; Sequence Homology, Amino Acid; Static Electricity; Two-Hybrid System Techniques
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