REVIEW: Molecular Architecture of Bacteriophage T4

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V. V. Mesyanzhinov^1*, 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

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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.

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

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