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-Structure paper
タイトル | The molecular architecture of the bacteriophage T4 neck. |
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ジャーナル・号・ページ | J Mol Biol, Vol. 425, Issue 10, Page 1731-1744, Year 2013 |
掲載日 | 2013年5月27日 |
著者 | Andrei Fokine / Zhihong Zhang / Shuji Kanamaru / Valorie D Bowman / Anastasia A Aksyuk / Fumio Arisaka / Venigalla B Rao / Michael G Rossmann / |
PubMed 要旨 | A hexamer of the bacteriophage T4 tail terminator protein, gp15, attaches to the top of the phage tail stabilizing the contractile sheath and forming the interface for binding of the independently ...A hexamer of the bacteriophage T4 tail terminator protein, gp15, attaches to the top of the phage tail stabilizing the contractile sheath and forming the interface for binding of the independently assembled head. Here we report the crystal structure of the gp15 hexamer, describe its interactions in T4 virions that have either an extended tail or a contracted tail, and discuss its structural relationship to other phage proteins. The neck of T4 virions is decorated by the "collar" and "whiskers", made of fibritin molecules. Fibritin acts as a chaperone helping to attach the long tail fibers to the virus during the assembly process. The collar and whiskers are environment-sensing devices, regulating the retraction of the long tail fibers under unfavorable conditions, thus preventing infection. Cryo-electron microscopy analysis suggests that twelve fibritin molecules attach to the phage neck with six molecules forming the collar and six molecules forming the whiskers. |
リンク | J Mol Biol / PubMed:23434847 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 2.7001 - 25.0 Å |
構造データ | EMDB-5528: Cryo-EM structure of the contracted bacteriophage T4 tail containing the collar and whiskers made of fibritin molecules. PDB-3j2m: PDB-3j2n: PDB-4hud: PDB-4huh: |
化合物 | ChemComp-HOH: |
由来 |
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キーワード | VIRAL PROTEIN / bacteriophage T4 / phage tail terminator protein / phage sheath protein / phage neck / collar whiskers / fibritin / gpwac / gp15 |