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.
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Dates
| Type | When |
|---|---|
| Created | 20 years, 10 months ago (Oct. 26, 2004, 5:49 p.m.) |
| Deposited | 3 years, 5 months ago (March 5, 2022, 3:54 a.m.) |
| Indexed | 1 week, 4 days ago (Aug. 24, 2025, 7:08 p.m.) |
| Issued | 20 years, 9 months ago (Nov. 15, 2004) |
| Published | 20 years, 9 months ago (Nov. 15, 2004) |
| Published Print | 20 years, 9 months ago (Nov. 15, 2004) |
@article{Trus_2004, title={Structure and Polymorphism of the UL6 Portal Protein of Herpes Simplex Virus Type 1}, volume={78}, ISSN={1098-5514}, url={http://dx.doi.org/10.1128/jvi.78.22.12668-12671.2004}, DOI={10.1128/jvi.78.22.12668-12671.2004}, number={22}, journal={Journal of Virology}, publisher={American Society for Microbiology}, author={Trus, Benes L. and Cheng, Naiqian and Newcomb, William W. and Homa, Fred L. and Brown, Jay C. and Steven, Alasdair C.}, year={2004}, month=nov, pages={12668–12671} }