1fgp: Difference between revisions
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[[ | ==MEMBRANE PENETRATION DOMAIN OF THE MINOR COAT PROTEIN G3P OF PHAGE FD, NMR, 15 STRUCTURES== | ||
<StructureSection load='1fgp' size='340' side='right' caption='[[1fgp]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1fgp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_fd Enterobacteria phage fd]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FGP FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fgp RCSB], [http://www.ebi.ac.uk/pdbsum/1fgp PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:9032075</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[G3p|G3p]] | *[[G3p|G3p]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Enterobacteria phage fd]] | [[Category: Enterobacteria phage fd]] | ||
[[Category: Holliger, P.]] | [[Category: Holliger, P.]] | ||
