1FGP
MEMBRANE PENETRATION DOMAIN OF THE MINOR COAT PROTEIN G3P OF PHAGE FD, NMR, 15 STRUCTURES
Summary for 1FGP
Entry DOI | 10.2210/pdb1fgp/pdb |
Descriptor | FD GENE 3 PROTEIN (1 entity in total) |
Functional Keywords | phage coat protein, sh3 domain, ph domain, pdz domain, fd phage, filamentous pahge, phage infection, ptb domain, viral protein |
Biological source | Enterobacteria phage fd |
Cellular location | Virion (Potential): P03661 |
Total number of polymer chains | 1 |
Total formula weight | 7711.48 |
Authors | Holliger, P.,Riechmann, L. (deposition date: 1996-12-10, release date: 1997-06-16, Last modification date: 2024-10-16) |
Primary citation | Holliger, P.,Riechmann, L. A conserved infection pathway for filamentous bacteriophages is suggested by the structure of the membrane penetration domain of the minor coat protein g3p from phage fd. Structure, 5:265-275, 1997 Cited by PubMed Abstract: . Gene 3 protein (g3p), a minor coat protein from bacteriophage fd mediates infection of Escherichia coli bearing an F-pilus. Its N-terminal domain (g3p-D1) is essential for infection and mediates penetration of the phage into the host cytoplasm presumbly through interaction with the Tol complex in the E. coli membranes. Structural knowledge of g3p-D1 is both important for a molecular understanding of phage infection and of biotechnological relevance, as g3p-D1 represents the primary fusion partner in phage display technology. PubMed: 9032075DOI: 10.1016/S0969-2126(97)00184-6 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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