Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA.
Lubkowski, J., Hennecke, F., Pluckthun, A., Wlodawer, A.(1999) Structure 7: 711-722
- PubMed: 10404600 
- DOI: https://doi.org/10.1016/s0969-2126(99)80092-6
- Primary Citation of Related Structures:  
1TOL - PubMed 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.
Organizational Affiliation: 
Macromolecular Structure Laboratory, NCI-Frederick Cancer Research and Development Center, MD 21702, USA. jacek@ncifcrf.gov