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Title | The tripartite capsid gene of Salmonella phage Gifsy-2 yields a capsid assembly pathway engaging features from HK97 and lambda. |
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Journal, issue, pages | Virology, Vol. 402, Issue 2, Page 355-365, Year 2010 |
Publish date | Jul 5, 2010 |
Authors | Grégory Effantin / Nara Figueroa-Bossi / Guy Schoehn / Lionello Bossi / James F Conway / |
PubMed Abstract | Phage Gifsy-2, a lambdoid phage infecting Salmonella, has an unusually large composite gene coding for its major capsid protein (mcp) at the C-terminal end, a ClpP-like protease at the N-terminus, ...Phage Gifsy-2, a lambdoid phage infecting Salmonella, has an unusually large composite gene coding for its major capsid protein (mcp) at the C-terminal end, a ClpP-like protease at the N-terminus, and a approximately 200 residue central domain of unknown function but which may have a scaffolding role. This combination of functions on a single coding region is more extensive than those observed in other phages such as HK97 (scaffold-capsid fusion) and lambda (protease-scaffold fusion). To study the structural phenotype of the unique Gifsy-2 capsid gene, we have purified Gifsy-2 particles and visualized capsids and procapsids by cryoelectron microscopy, determining structures to resolutions up to 12A. The capsids have lambdoid T=7 geometry and are well modeled with the atomic structures of HK97 mcp and phage lambda gpD decoration protein. Thus, the unique Gifsy-2 capsid protein gene yields a capsid maturation pathway engaging features from both phages HK97 and lambda. |
External links | Virology / PubMed:20427067 |
Methods | EM (single particle) |
Resolution | 11.8 - 25.6 Å |
Structure data | EMDB-1691: EMDB-1692: EMDB-1693: EMDB-1694: |