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REVIEW: Molecular Architecture of Bacteriophage T4

V. V. Mesyanzhinov1*, P. G. Leiman2, V. A. Kostyuchenko1, L. P. Kurochkina1, K. A. Miroshnikov1, N. N. Sykilinda1, and M. M. Shneider1

1Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow 117997, Russia; fax: (7-095) 336-6022; E-mail: vvm@ibch.ru

2Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-1392, USA; fax: +1 (765) 496-1189; E-mail: leiman@purdue.edu

* To whom correspondence should be addressed.

Received July 9, 2004
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.
KEY WORDS: bacteriophage T4, baseplate, tail sheath, infection mechanisms, virus structure, protein structure, cryo-electron microscopy, X-ray analysis, 3D reconstruction