The molecular architecture of the bacteriophage T4 neck.

The molecular architecture of the bacteriophage T4 neck.
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DOI:
10.1016/j.jmb.2013.02.012
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发表时间:
2013-05-27
影响因子:
5.6
通讯作者:
Rossmann, Michael G.
Rossmann, Michael G.
中科院分区:
生物学2区
文献类型:
--
作者:
Fokine, Andrei;Zhang, Zhihong;Kanamaru, Shuji;Bowman, Valorie D.;Aksyuk, Anastasia A.;Arisaka, Fumio;Rao, Venigalla B.;Rossmann, Michael G.

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噬菌体T4尾部终止子蛋白的六聚体gp15附着于噬菌体尾部的顶部,稳定可收缩鞘并形成用于结合独立组装的头部的界面。在这里,我们报告的gp15六聚体的晶体结构,描述其在T4病毒体,有一个延长的尾巴或收缩的尾巴,并讨论其结构关系到其他噬菌体蛋白的相互作用。T4病毒粒子的颈部由纤维蛋白分子组成的“衣领”和“胡须”装饰。纤维蛋白作为一种分子伴侣,在装配过程中帮助将长尾纤维附着到病毒上。项圈和触须是环境感应装置,在不利条件下调节长尾纤维的收缩,从而防止感染。冷冻电子显微镜分析表明,12个纤维蛋白分子附着在噬菌体颈部,其中6个分子形成衣领,6个分子形成胡须。
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.
DOI: 10.1073/pnas.0400444101
发表时间: 2004-04-20
影响因子: 11.1
作者:
Fokine, A;Chipman, PR;Rossmann, MG
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期刊: STRUCTURE
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