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-Structure paper
タイトル | The tail structure of bacteriophage T4 and its mechanism of contraction. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 12, Issue 9, Page 810-813, Year 2005 |
掲載日 | 2005年8月14日 |
著者 | Victor A Kostyuchenko / Paul R Chipman / Petr G Leiman / Fumio Arisaka / Vadim V Mesyanzhinov / Michael G Rossmann / |
PubMed 要旨 | Bacteriophage T4 and related viruses have a contractile tail that serves as an efficient mechanical device for infecting bacteria. A three-dimensional cryo-EM reconstruction of the mature T4 tail ...Bacteriophage T4 and related viruses have a contractile tail that serves as an efficient mechanical device for infecting bacteria. A three-dimensional cryo-EM reconstruction of the mature T4 tail assembly at 15-A resolution shows the hexagonal dome-shaped baseplate, the extended contractile sheath, the long tail fibers attached to the baseplate and the collar formed by six whiskers that interact with the long tail fibers. Comparison with the structure of the contracted tail shows that tail contraction is associated with a substantial rearrangement of the domains within the sheath protein and results in shortening of the sheath to about one-third of its original length. During contraction, the tail tube extends beneath the baseplate by about one-half of its total length and rotates by 345 degrees , allowing it to cross the host's periplasmic space. |
リンク | Nat Struct Mol Biol / PubMed:16116440 |
手法 | EM (単粒子) / EM (らせん対称) |
解像度 | 15.0 Å |
構造データ | EMDB-1126: The tail structure of bacteriophage T4 and its mechanism of contraction. |
化合物 | ChemComp-EPE: |
由来 |
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キーワード | VIRAL PROTEIN (ウイルスタンパク質) / Structural protein (タンパク質) / ATTACHMENT PROTEIN / BACTERIOPHAGE ASSEMBLY (ファージ) / BACTERIOPHAGE T4 (T4ファージ) / CHAPERONE (シャペロン) / FIBRITIN |