1TOL

FUSION OF N-TERMINAL DOMAIN OF THE MINOR COAT PROTEIN FROM GENE III IN PHAGE M13, AND C-TERMINAL DOMAIN OF E. COLI PROTEIN-TOLA

Summary for 1TOL

• Entry DOI: 10.2210/pdb1tol/pdb
• Descriptor: PROTEIN (FUSION PROTEIN CONSISTING OF MINOR COAT PROTEIN, GLYCINE RICH LINKER, TOLA, AND A HIS TAG) (2 entities in total)
• Functional Keywords: bacteriophage m13, phage infection, tol pathway, fusion protein, viral protein
• Biological source: Enterobacteria phage M13; More
• Cellular location: Cell inner membrane; Single-pass type II membrane protein: P19934
• Total number of polymer chains: 1
• Total formula weight: 22851.12

Authors

Lubkowski, J.,Wlodawer, A.,Hennecke, F.,Plueckthun, A. (deposition date: 1999-05-17, release date: 1999-05-20, Last modification date: 2024-10-30)

Primary citation

Lubkowski, J.,Hennecke, F.,Pluckthun, A.,Wlodawer, A.
Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA.
Structure Fold.Des., 7:711-722, 1999

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.

PubMed: 10404600
DOI: 10.1016/S0969-2126(99)80092-6

Experimental method

X-RAY DIFFRACTION (1.85 Å)