Mesyanzhinov V V, Leiman P G, Kostyuchenko V A, Kurochkina L P, Miroshnikov K A, Sykilinda N N, Shneider M M
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.
Biochemistry (Mosc). 2004 Nov;69(11):1190-202. doi: 10.1007/s10541-005-0064-9.
In studying bacteriophage T4--one of the basic models of molecular biology for several decades--there has come a Renaissance, and this virus is now actively used as object of structural biology. The structures of six proteins of the phage particle have recently been determined at atomic resolution by X-ray crystallography. Three-dimensional reconstruction of the infection device--one of the most complex multiprotein components--has been developed on the basis of cryo-electron microscopy images. The further study of bacteriophage T4 structure will allow a better understanding of the regulation of protein folding, assembly of biological structures, and also mechanisms of functioning of the complex biological molecular machines.
在研究噬菌体T4（几十年来分子生物学的基本模型之一）方面，出现了复兴，这种病毒现在正被积极用作结构生物学的研究对象。最近，通过X射线晶体学已在原子分辨率下确定了噬菌体颗粒六种蛋白质的结构。基于冷冻电子显微镜图像，已开发出感染装置（最复杂的多蛋白组件之一）的三维重建。对噬菌体T4结构的进一步研究将有助于更好地理解蛋白质折叠的调控、生物结构的组装以及复杂生物分子机器的功能机制。
