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'''MEMBRANE PENETRATION DOMAIN OF THE MINOR COAT PROTEIN G3P OF PHAGE FD, NMR, 15 STRUCTURES''' | '''MEMBRANE PENETRATION DOMAIN OF THE MINOR COAT PROTEIN G3P OF PHAGE FD, NMR, 15 STRUCTURES''' | ||
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[[Category: Holliger, P.]] | [[Category: Holliger, P.]] | ||
[[Category: Riechmann, L.]] | [[Category: Riechmann, L.]] | ||
[[Category: | [[Category: Fd phage]] | ||
[[Category: | [[Category: Filamentous pahge]] | ||
[[Category: | [[Category: Pdz domain]] | ||
[[Category: | [[Category: Ph domain]] | ||
[[Category: | [[Category: Phage coat protein]] | ||
[[Category: | [[Category: Phage infection]] | ||
[[Category: | [[Category: Ptb domain]] | ||
[[Category: | [[Category: Sh3 domain]] | ||
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Revision as of 16:18, 2 May 2008
MEMBRANE PENETRATION DOMAIN OF THE MINOR COAT PROTEIN G3P OF PHAGE FD, NMR, 15 STRUCTURES
OverviewOverview
BACKGROUND:. 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. RESULTS:. The solution structure of g3p-D1 was determined by NMR spectroscopy. The principal structural element of g3p-D1 is formed by a six-stranded beta barrel topologically identical to a permutated SH3 domain but capped by an additional N-terminal alpha helix. The presence of structurally similar domains in the related E. coli phages, lke and 12-2, as well as in the cholera toxin transducing phage ctxφ is indicated. The structure of g3p-D1 resembles those of the recently described PTB and PDZ domains involved in eukaryotic signal transduction. CONCLUSIONS:. The predicted presence of similar structures in membrane penetration domains from widely diverging filamentous phages suggests they share a conserved infection pathway. The widespread hydrogen-bond network within the beta barrel and N-terminal alpha helix in combination with two disulphide bridges renders g3p-D1 a highly stable domain, which may be important for keeping phage infective in harsh extracellular environments.
About this StructureAbout this Structure
1FGP is a Single protein structure of sequence from Enterobacteria phage fd. Full crystallographic information is available from OCA.
ReferenceReference
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., Holliger P, Riechmann L, Structure. 1997 Feb 15;5(2):265-75. PMID:9032075 Page seeded by OCA on Fri May 2 16:18:18 2008