3nb3

From Proteopedia

(Difference between revisions)

Revision as of 18:40, 10 April 2020

The host outer membrane proteins OmpA and OmpC are packed at specific sites in the Shigella phage Sf6 virion as structural components

3nb3, resolution 19.00Å

Structural highlights

3nb3 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1qjp, 2j1n
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[OMPA_ECOLI] Required for the action of colicins K and L and for the stabilization of mating aggregates in conjugation. Serves as a receptor for a number of T-even like phages. Also acts as a porin with low permeability that allows slow penetration of small solutes. [OMPC_ECOLI] Forms pores that allow passive diffusion of small molecules across the outer membrane.

Publication Abstract from PubMed

Assembly of dsDNA bacteriophage is a precisely programmed process. Potential roles of host cell components in phage assembly haven't been well understood. It was previously reported that two unidentified proteins were present in bacteriophage Sf6 virion (Casjens et al, 2004, J.Mol.Biol. 339, 379-394, Fig. 2A). Using tandem mass spectrometry, we have identified the two proteins as outer membrane proteins (OMPs) OmpA and OmpC from its host Shigella flexneri. The transmission electron cryo-microscopy structure of Sf6 shows significant density at specific sites at the phage capsid inner surface. This density fit well with the characteristic beta-barrel domains of OMPs, thus may be due to the two host proteins. Locations of this density suggest a role in Sf6 morphogenesis reminiscent of phage-encoded cementing proteins. These data indicate a new, OMP-related phage:host linkage, adding to previous knowledge that some lambdoid bacteriophage genomes contain OmpC-like genes that express phage-encoded porins in the lysogenic state.

The host outer membrane proteins OmpA and OmpC are associated with the Shigella phage Sf6 virion.,Zhao H, Sequeira RD, Galeva NA, Tang L Virology. 2011 Jan 20;409(2):319-27. Epub 2010 Nov 10. PMID:21071053^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zhao H, Sequeira RD, Galeva NA, Tang L. The host outer membrane proteins OmpA and OmpC are associated with the Shigella phage Sf6 virion. Virology. 2011 Jan 20;409(2):319-27. Epub 2010 Nov 10. PMID:21071053 doi:10.1016/j.virol.2010.10.030

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3nb3"

@@ Line 3: / Line 3: @@
 <SX load='3nb3' size='340' side='right' viewer='molstar' caption='[[3nb3]], [[Resolution|resolution]] 19.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3nb3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NB3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NB3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3nb3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NB3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3NB3 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qjp|1qjp]], [[2j1n|2j1n]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nb3 OCA], [http://pdbe.org/3nb3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nb3 RCSB], [http://www.ebi.ac.uk/pdbsum/3nb3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nb3 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3nb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nb3 OCA], [http://pdbe.org/3nb3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nb3 RCSB], [http://www.ebi.ac.uk/pdbsum/3nb3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nb3 ProSAT]</span></td></tr>
 </table>
 == Function ==

3nb3

From Proteopedia

Revision as of 18:40, 10 April 2020

The host outer membrane proteins OmpA and OmpC are packed at specific sites in the Shigella phage Sf6 virion as structural components

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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