title: The beta-prism: a new folding motif.
abstract: A new protein fold with internal symmetry has been observed in two proteins: vitelline membrane outer layer protein I (VMO-I) and delta-endotoxin. Despite lacking any discernible sequence similarity, both proteins have similar three-dimensional structures as well as a carbohydrate-binding site in the top region of the common fold.
authors.affiliation: Nara Institute of Science and Technology, Japan. shimizu@bs.aist-nara.ac.jp
authors.forename: T
authors.initials: T
authors.lastname: Shimizu
authors.forename: K
authors.initials: K
authors.lastname: Morikawa
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001427:Bacterial Toxins; D001717:Birds; D004527:Egg Proteins / Q000737:chemistry / Q000378:metabolism*; D004731:Endotoxins / Q000737:chemistry / Q000378:metabolism*; D006460:Hemolysin Proteins; D008969:Molecular Sequence Data; D017510:Protein Folding
chemical_list: D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004527:Egg Proteins; D004731:Endotoxins; D006460:Hemolysin Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis; C035651:vitelline membrane proteins