Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1.
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ABSTRACT:
SUBMITTER: Trus BL
PROVIDER: S-EPMC525097 | biostudies-literature | 2004 Nov
REPOSITORIES: biostudies-literature
Publications
Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1.
Trus Benes L BL Cheng Naiqian N Newcomb William W WW Homa Fred L FL Brown Jay C JC Steven Alasdair C AC
Journal of virology 20041101 22
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 A, it has an axial channel, peripheral flanges, and fits snugly into a vacant vertex site. Its architecture resembles those of bacteriophage portal/connector proteins. ...[more]
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