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-Structure paper
タイトル | The PM2 virion has a novel organization with an internal membrane and pentameric receptor binding spikes. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 11, Issue 9, Page 850-856, Year 2004 |
掲載日 | 2004年8月1日 |
著者 | Juha T Huiskonen / Hanna M Kivelä / Dennis H Bamford / Sarah J Butcher / |
PubMed 要旨 | Biological membranes are notoriously resistant to structural analysis. Excellent candidates to tackle this problem in situ are membrane-containing viruses where the membrane is constrained by an ...Biological membranes are notoriously resistant to structural analysis. Excellent candidates to tackle this problem in situ are membrane-containing viruses where the membrane is constrained by an icosahedral capsid. Cryo-EM and image reconstruction of bacteriophage PM2 revealed a membrane bilayer following the internal surface of the capsid. The viral genome closely interacts with the inner leaflet. The capsid, at a resolution of 8.4 A, reveals 200 trimeric capsomers with a pseudo T = 21 dextro organization. Pentameric receptor-binding spikes protrude from the surface. It is evident from the structure that the PM2 membrane has at least two important roles in the life cycle. First, it acts as a scaffold to nucleate capsid assembly. Second, after host recognition, it fuses with the host outer membrane to promote genome entry. The structure also sheds light on how the viral supercoiled circular double-stranded DNA genome might be packaged and released. |
リンク | Nat Struct Mol Biol / PubMed:15286721 |
手法 | EM (単粒子) |
解像度 | 8.4 - 13.4 Å |
構造データ | EMDB-1082: EMDB-1083: EMDB-1084: EMDB-1085: |