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Science 5 May 2000:
Vol. 288. no. 5467, pp. 877 - 880
DOI: 10.1126/science.288.5467.877
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Reports

Seeing the Herpesvirus Capsid at 8.5 Å 

Z. Hong Zhou, 1 Matthew Dougherty, 2 Joanita Jakana, 2 Jing He, 3 Frazer J. Rixon, 4 Wah Chiu 23*

Human herpesviruses are large and structurally complex viruses that cause a variety of diseases. The three-dimensional structure of the herpesvirus capsid has been determined at 8.5 angstrom resolution by electron cryomicroscopy. More than 30 putative alpha helices were identified in the four proteins that make up the 0.2 billion-dalton shell. Some of these helices are located at domains that undergo conformational changes during capsid assembly and DNA packaging. The unique spatial arrangement of the heterotrimer at the local threefold positions accounts for the asymmetric interactions with adjacent capsid components and the unusual co-dependent folding of its subunits.

1 Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, TX 77030, USA.
2 National Center for Macromolecular Imaging, Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
3 Graduate Program in Structural and Computational Biology and Molecular Biophysics, Baylor College of Medicine, Houston, TX 77030, USA.
4 MRC Virology Unit, Institute of Virology, Glasgow G11 5JR, Scotland, UK.
*   To whom correspondence should be addressed. E-mail: wah{at}bcm.tmc.edu

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