title: Three-dimensional structure of the bacteriophage P22 tail machine.
abstract: The tail of the bacteriophage P22 is composed of multiple protein components and integrates various biological functions that are crucial to the assembly and infection of the phage. The three-dimensional structure of the P22 tail machine determined by electron cryo-microscopy and image reconstruction reveals how the five types of polypeptides present as 51 subunits are organized into this molecular machine through twelve-, six- and three-fold symmetry, and provides insights into molecular events during host cell attachment and phage DNA translocation.
authors.affiliation: Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
authors.forename: Liang
authors.initials: L
authors.lastname: Tang
authors.forename: William R
authors.initials: WR
authors.lastname: Marion
authors.forename: Gino
authors.initials: G
authors.lastname: Cingolani
authors.forename: Peter E
authors.initials: PE
authors.lastname: Prevelige
authors.forename: John E
authors.initials: JE
authors.lastname: Johnson
mesh_terms: D000595:Amino Acid Sequence; D017100:Bacteriophage P22 / Q000737:chemistry* / Q000235:genetics; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D005583:Fourier Analysis; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017376:Viral Tail Proteins / Q000737:chemistry* / Q000235:genetics
chemical_list: D017376:Viral Tail Proteins