1fgp: Difference between revisions

Line 1:

[[Image:1fgp.gif|left|200px]]<br /><applet load="1fgp" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1fgp.gif|left|200px]]<br /><applet load="1fgp" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1fgp" />

'''MEMBRANE PENETRATION DOMAIN OF THE MINOR COAT PROTEIN G3P OF PHAGE FD, NMR, 15 STRUCTURES'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1FGP OCA].

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==

Line 24:

[[Category: sh3 domain]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 14~~:54:~~38 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:28 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1fgp.gif|left|200px]]<br /><applet load="1fgp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fgp.gif|left|200px]]<br /><applet load="1fgp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fgp" />
 '''MEMBRANE PENETRATION DOMAIN OF THE MINOR COAT PROTEIN G3P OF PHAGE FD, NMR, 15 STRUCTURES'''<br />
 ==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 ctx&phi; 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.
+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 ctx&phi; 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==
-FGP 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FGP OCA].
+FGP 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==
@@ Line 24: / Line 24: @@
 [[Category: sh3 domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:54:38 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:28 2008''