spacer Fitting of the gp6 crystal structure into 3D cryo-EM reconstruction of bacteriophage T4 dome-shaped baseplate
Primary citation
Title The structure of gene product 6 of bacteriophage T4, the hinge-pin of the baseplate.
Authors Aksyuk,; Leiman,; Shneider,; Mesyanzhinov,; Rossmann,
Journal STRUCTUREsearch vol:17, pag:800-808 (2009), Identifiers: PubMed ID (19523898)search DOI (10.1016/j.str.2009.04.005)
Abstract The baseplate of bacteriophage T4 is a multicomponent protein complex, which controls phage attachment to the host. It assembles from six wedges and a central hub. During infection the baseplate undergoes a large conformational change from a dome-shaped to a flat, star-shaped structure. We report the crystal structure of the C-terminal half of gene product (gp) 6 and investigate its motion with respect to the other proteins during the baseplate rearrangement. Six gp6 dimers interdigitate, forming a ring that maintains the integrity of the baseplate in both conformations. One baseplate wedge contains an N-terminal dimer of gp6, whereas neighboring wedges are tied together through the C-terminal dimer of gp6. The dimeric interactions are preserved throughout the rearrangement of the baseplate. However, the hinge angle between the N- and C-terminal parts of gp6 changes by approximately 15 degrees , accounting for a 10 A radial increase in the diameter of the gp6 ring.
MeSH terms Amino Acid Sequencesearch, Bacteriophage T4search, Cryoelectron Microscopysearch, Crystallizationsearch, Dimerizationsearch, Genessearch, Viralsearch, Glycoproteinssearch, Modelssearch, Molecularsearch, Molecular Sequence Datasearch, Protein Conformationsearch, Protein Structuresearch, Secondarysearch, Protein Structuresearch, Tertiarysearch, Viral Proteinssearch
Other entries described in this publication 3h2t, 3h3y