title: The crystal structure of lysin, a fertilization protein.
abstract: Lysin, a protein from abalone sperm, creates a hole in the envelope of the egg, permitting the sperm to pass through the envelope and fuse with the egg. The structure of lysin, refined at 1.9 angstroms resolution, reveals an alpha-helical, amphipathic molecule. The surface of the protein exhibits three features: two tracks of basic residues that span the length of the molecule, a solvent-exposed cluster of aromatic and aliphatic amino acids, and an extended amino-terminal hypervariable domain that is species-specific. The structure suggests possible mechanisms of action.
authors.affiliation: Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037-1093.
authors.forename: A
authors.initials: A
authors.lastname: Shaw
authors.forename: D E
authors.initials: DE
authors.lastname: McRee
authors.forename: V D
authors.initials: VD
authors.lastname: Vacquier
authors.forename: C D
authors.initials: CD
authors.lastname: Stout
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008974:Mollusca; D009088:Mucoproteins / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary; D014817:Vitelline Membrane / Q000378:metabolism
chemical_list: D009088:Mucoproteins; C010393:lysin, gastropoda