title: Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1.
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 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.
authors.affiliation: 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.
authors.forename: Benes L
authors.initials: BL
authors.lastname: Trus
authors.forename: Naiqian
authors.initials: N
authors.lastname: Cheng
authors.forename: William W
authors.initials: WW
authors.lastname: Newcomb
authors.forename: Fred L
authors.initials: FL
authors.lastname: Homa
authors.forename: Jay C
authors.initials: JC
authors.lastname: Brown
authors.forename: Alasdair C
authors.initials: AC
authors.lastname: Steven
mesh_terms: D036022:Capsid Proteins / Q000737:chemistry*; D021621:Imaging, Three-Dimensional; D008854:Microscopy, Electron; D011110:Polymorphism, Genetic; D014764:Viral Proteins
chemical_list: D036022:Capsid Proteins; D014764:Viral Proteins; C069185:DNA cleavage and packaging proteins, Herpesvirus