Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1.
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.
Trus
Benes L
BL
Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Building 50, Room 1517, MSC 8025, 50 South Drive, Bethesda, MD 20892-8025, USA.
Cheng
Naiqian
N
Newcomb
William W
WW
Homa
Fred L
FL
Brown
Jay C
JC
Steven
Alasdair C
AC
D036022:Capsid Proteins / Q000737:chemistry*; D021621:Imaging, Three-Dimensional; D008854:Microscopy, Electron; D011110:Polymorphism, Genetic; D014764:Viral Proteins
D036022:Capsid Proteins; D014764:Viral Proteins; C069185:DNA cleavage and packaging proteins, Herpesvirus