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-Structure paper
| タイトル | The tripartite capsid gene of Salmonella phage Gifsy-2 yields a capsid assembly pathway engaging features from HK97 and lambda. |
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| ジャーナル・号・ページ | Virology, Vol. 402, Issue 2, Page 355-365, Year 2010 |
| 掲載日 | 2010年7月5日 |
著者 | Grégory Effantin / Nara Figueroa-Bossi / Guy Schoehn / Lionello Bossi / James F Conway / ![]() |
| PubMed 要旨 | 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. |
リンク | Virology / PubMed:20427067 |
| 手法 | EM (単粒子) |
| 解像度 | 11.8 - 25.6 Å |
| 構造データ | ![]() EMDB-1691: ![]() EMDB-1692: ![]() EMDB-1693: ![]() EMDB-1694: |
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