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-Structure paper
タイトル | Peering down the barrel of a bacteriophage portal: the genome packaging and release valve in p22. |
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ジャーナル・号・ページ | Structure, Vol. 19, Issue 4, Page 496-502, Year 2011 |
掲載日 | 2011年4月13日 |
著者 | Jinghua Tang / Gabriel C Lander / Adam S Olia / Rui Li / Sherwood Casjens / Peter Prevelige / Gino Cingolani / Timothy S Baker / John E Johnson / |
PubMed 要旨 | The encapsidated genome in all double-strand DNA bacteriophages is packaged to liquid crystalline density through a unique vertex in the procapsid assembly intermediate, which has a portal protein ...The encapsidated genome in all double-strand DNA bacteriophages is packaged to liquid crystalline density through a unique vertex in the procapsid assembly intermediate, which has a portal protein dodecamer in place of five coat protein subunits. The portal orchestrates DNA packaging and exit, through a series of varying interactions with the scaffolding, terminase, and closure proteins. Here, we report an asymmetric cryoEM reconstruction of the entire P22 virion at 7.8 Å resolution. X-ray crystal structure models of the full-length portal and of the portal lacking 123 residues at the C terminus in complex with gene product 4 (Δ123portal-gp4) obtained by Olia et al. (2011) were fitted into this reconstruction. The interpreted density map revealed that the 150 Å, coiled-coil, barrel portion of the portal entraps the last DNA to be packaged and suggests a mechanism for head-full DNA signaling and transient stabilization of the genome during addition of closure proteins. |
リンク | Structure / PubMed:21439834 / PubMed Central |
手法 | EM (単粒子) |
構造データ | EMDB-5231: EMDB-5232: EMDB-5348: |