3NB3
The host outer membrane proteins OmpA and OmpC are packed at specific sites in the Shigella phage Sf6 virion as structural components
Summary for 3NB3
| Entry DOI | 10.2210/pdb3nb3/pdb |
| Related | 1qjp 2J1N |
| EMDB information | 5201 |
| Descriptor | Outer membrane protein A, Outer membrane protein C (2 entities in total) |
| Functional Keywords | virus assembly, cementing protein, bacteriophage, sf6, shigella, beta-barrel, outer membrane protein, icosahedral, membrane protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 150154.26 |
| Authors | Zhao, H.,Sequeira, R.D.,Galeva, N.A.,Tang, L. (deposition date: 2010-06-02, release date: 2011-02-16, Last modification date: 2024-02-21) |
| Primary citation | Zhao, H.,Sequeira, R.D.,Galeva, N.A.,Tang, L. The host outer membrane proteins OmpA and OmpC are associated with the Shigella phage Sf6 virion. Virology, 409:319-327, 2011 Cited by PubMed Abstract: 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. PubMed: 21071053DOI: 10.1016/j.virol.2010.10.030 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (19 Å) |
Structure validation
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