Clusters in an intrinsically disordered protein create a protein-binding site: the TolB-binding region of colicin E9.

Journal article

The 61-kDa colicin E9 protein toxin enters the cytoplasm of susceptible cells by interacting with outer membrane and periplasmic helper proteins and kills them by hydrolyzing their DNA. The membrane translocation function is located in the N-terminal domain of the colicin, with a key signal sequence being a pentapeptide region that governs the interaction with the helper protein TolB (the TolB box). Previous NMR studies [Collins et al. (2002) J. Mol. Biol. 318, 787-904; MacDonald et al. (2004...

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Authors: Tozawa, K; Macdonald, C; Penfold, C; James, R; Kleanthous, K

• Journal: Biochemistry
• Volume: 44
• Issue: 34
• Pages: 11496-11507
• Publication date: 2005-08-01
• DOI: 10.1021/bi0503596
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Molecular Sequence Data; Amino Acid Substitution; Mutagenesis, Site-Directed; Escherichia coli; Structure-Activity Relationship; Recombinant Fusion Proteins; Binding Sites; Periplasmic Proteins; Colicins; Amino Acid Sequence; Escherichia coli Proteins