PMID:10404600
| Citation |
Lubkowski, J, Hennecke, F, Plückthun, A and Wlodawer, A (1999) Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA. Structure 7:711-22 |
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| Abstract |
Infection of male Escherichia coli cells by filamentous Ff bacteriophages (M13, fd, and f1) involves interaction of the phage minor coat gene 3 protein (g3p) with the bacterial F pilus (primary receptor), and subsequently with the integral membrane protein TolA (coreceptor). G3p consists of three domains (N1, N2, and CT). The N2 domain interacts with the F pilus, whereas the N1 domain--connected to N2 by a flexible glycine-rich linker and tightly interacting with it on the phage--forms a complex with the C-terminal domain of TolA at later stages of the infection process. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacteriophages/pathogenicity; Capsid/chemistry; Capsid Proteins; Crystallography, X-Ray; Escherichia coli/virology; Escherichia coli Proteins; Models, Molecular; Molecular Sequence Data; Peptide Fragments/chemistry; Protein Folding; Protein Structure, Secondary |
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