title: The filamentous phage pIV multimer visualized by scanning transmission electron microscopy.
abstract: A family of homomultimeric outer-membrane proteins termed secretins mediates the secretion of large macromolecules such as enzymes and filamentous bacteriophages across bacterial outer membranes to the extracellular milieu. The secretin encoded by filamentous phage f1 was purified. Mass determination of individual molecules by scanning transmission electron microscopy revealed two forms, a unit multimer composed of about 14 subunits and a multimer dimer. The secretin is roughly cylindrical and has an internal diameter of about 80 angstroms, which is large enough to accommodate filamentous phage (diameter of 65 angstroms).
authors.affiliation: Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
authors.forename: N A
authors.initials: NA
authors.lastname: Linderoth
authors.forename: M N
authors.initials: MN
authors.lastname: Simon
authors.forename: M
authors.initials: M
authors.lastname: Russel
mesh_terms: D001704:Biopolymers; D003090:Coliphages / Q000737:chemistry*; D004396:Coloring Agents; D019281:Dimerization; D008744:Methylamines; D017348:Microscopy, Electron, Scanning Transmission; D008970:Molecular Weight; D011487:Protein Conformation; D012995:Solubility; D014638:Vanadates; D014764:Viral Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000648:ultrastructure*
chemical_list: D001704:Biopolymers; D004396:Coloring Agents; D008744:Methylamines; D014764:Viral Proteins; D014638:Vanadates; C027451:methylamine