Structure and Polymorphism of the UL6 Portal Protein of Herpes Simplex Virus Type 1

Author:

Trus Benes L.12,Cheng Naiqian2,Newcomb William W.3,Homa Fred L.4,Brown Jay C.3,Steven Alasdair C.2

Affiliation:

1. Imaging Sciences Laboratory, Division of Computational Bioscience, Center for Information Technology

2. Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland

3. Department of Microbiology and Cancer Center, University of Virginia Health System, Charlottesville, Virginia

4. Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania

Abstract

ABSTRACT By electron microscopy and image analysis, we find that baculovirus-expressed UL6 is polymorphic, consisting of rings of 11-, 12-, 13-, and 14-fold symmetry. The 12-mer is likely to be the oligomer incorporated into procapsids: at a resolution of 16 Å, it has an axial channel, peripheral flanges, and fits snugly into a vacant vertex site. Its architecture resembles those of bacteriophage portal/connector proteins.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Reference21 articles.

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2. Black, L. W., M. K. Showe, and A. C. Steven. 1994. Morphogenesis of the T4 head, p. 218-258. In J. Karam (ed.), Molecular biology of bacteriophage T4. American Society for Microbiology, Washington, D.C.

3. Cerritelli, M. E., J. F. Conway, N. Cheng, B. L. Trus, and A. C. Steven. 2002. Molecular mechanisms in bacteriophage T7 assembly, maturation and DNA containment. Adv. Protein Chem.64:301-323.

4. Handedness of the Herpes Simplex Virus Capsid and Procapsid

5. Cingolani, G., S. D. Moore, P. E. J. Prevelige, and J. E. Johnson. 2002. Preliminary crystallographic analysis of the bacteriophage P22 portal protein. J. Struct. Biol.277:20794-20803.

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