title: Identification of additional coat-scaffolding interactions in a bacteriophage P22 mutant defective in maturation.
abstract: Scaffolding proteins play a critical role in the assembly of certain viruses by directing the formation and maturation of a precursor capsid. Using electron cryomicroscopy difference mapping, we have identified an altered arrangement of a mutant scaffolding within the bacteriophage P22 procapsid. This mutant scaffolding allows us to directly visualize scaffolding density within the P22 procapsid. Based on these observations we propose a model for why the mutant prevents scaffolding release and capsid maturation.
authors.affiliation: Verna and Marrs McLean, Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030, USA.
authors.forename: P A
authors.initials: PA
authors.lastname: Thuman-Commike
authors.forename: B
authors.initials: B
authors.lastname: Greene
authors.forename: J
authors.initials: J
authors.lastname: Jakana
authors.forename: A
authors.initials: A
authors.lastname: McGough
authors.forename: P E
authors.initials: PE
authors.lastname: Prevelige
authors.forename: W
authors.initials: W
authors.lastname: Chiu
mesh_terms: D017100:Bacteriophage P22 / Q000235:genetics* / Q000254:growth & development* / Q000378:metabolism; D002213:Capsid / Q000378:metabolism*; D020285:Cryoelectron Microscopy; D009154:Mutation; D011498:Protein Precursors / Q000378:metabolism*; D015678:Viral Structural Proteins / Q000378:metabolism*
chemical_list: D011498:Protein Precursors; D015678:Viral Structural Proteins; C111088:scaffolding protein, bacteriophage P22