1fgp
From Proteopedia
(New page: 200px<br /><applet load="1fgp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fgp" /> '''MEMBRANE PENETRATION DOMAIN OF THE MINOR COA...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1fgp.gif|left|200px]]<br /><applet load="1fgp" size=" | + | [[Image:1fgp.gif|left|200px]]<br /><applet load="1fgp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fgp" /> | caption="1fgp" /> | ||
'''MEMBRANE PENETRATION DOMAIN OF THE MINOR COAT PROTEIN G3P OF PHAGE FD, NMR, 15 STRUCTURES'''<br /> | '''MEMBRANE PENETRATION DOMAIN OF THE MINOR COAT PROTEIN G3P OF PHAGE FD, NMR, 15 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND:. Gene 3 protein (g3p), a minor coat protein from bacteriophage | + | 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 Structure== | ==About this Structure== | ||
| - | 1FGP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phage_phi3t Phage phi3t]. Full crystallographic information is available from [http:// | + | 1FGP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phage_phi3t Phage phi3t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGP OCA]. |
==Reference== | ==Reference== | ||
| Line 24: | Line 24: | ||
[[Category: sh3 domain]] | [[Category: sh3 domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:28 2008'' |
Revision as of 10:38, 21 February 2008
|
MEMBRANE PENETRATION DOMAIN OF THE MINOR COAT PROTEIN G3P OF PHAGE FD, NMR, 15 STRUCTURES
Overview
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 Structure
1FGP is a Single protein structure of sequence from Phage phi3t. Full crystallographic information is available from OCA.
Reference
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 Thu Feb 21 12:38:28 2008
