+検索条件
-Structure paper
タイトル | The tail sheath structure of bacteriophage T4: a molecular machine for infecting bacteria. |
---|---|
ジャーナル・号・ページ | EMBO J, Vol. 28, Issue 7, Page 821-829, Year 2009 |
掲載日 | 2009年4月8日 |
著者 | Anastasia A Aksyuk / Petr G Leiman / Lidia P Kurochkina / Mikhail M Shneider / Victor A Kostyuchenko / Vadim V Mesyanzhinov / Michael G Rossmann / |
PubMed 要旨 | The contractile tail of bacteriophage T4 is a molecular machine that facilitates very high viral infection efficiency. Its major component is a tail sheath, which contracts during infection to less ...The contractile tail of bacteriophage T4 is a molecular machine that facilitates very high viral infection efficiency. Its major component is a tail sheath, which contracts during infection to less than half of its initial length. The sheath consists of 138 copies of the tail sheath protein, gene product (gp) 18, which surrounds the central non-contractile tail tube. The contraction of the sheath drives the tail tube through the outer membrane, creating a channel for the viral genome delivery. A crystal structure of about three quarters of gp18 has been determined and was fitted into cryo-electron microscopy reconstructions of the tail sheath before and after contraction. It was shown that during contraction, gp18 subunits slide over each other with no apparent change in their structure. |
リンク | EMBO J / PubMed:19229296 / PubMed Central |
手法 | X線回折 / EM (単粒子) |
解像度 | 1.8 - 16 Å |
構造データ | PDB-3fo8: PDB-3foa: PDB-3foh: PDB-3foi: |
化合物 | ChemComp-ACT: ChemComp-HOH: |
由来 |
|
キーワード | VIRAL PROTEIN / mostly beta / viral structural protein / bacteriophage T4 / tail sheath / alpha-beta |