title: Primary structure of two cytolysin isoforms from Stichodactyla helianthus differing in their hemolytic activity.
abstract: Sticholysin I (St-I) and sticholysin II (St-II) are cytolysins purified from the sea anemone Stichodactyla helianthus with a high degree of sequence identity (93%) but clearly differenced in their hemolytic activity. In order to go further into the structural determinants for the different behavior of St-I and St-II, we report here the complete amino acid sequences and the consensus secondary structure prediction of both proteins. The complete determination of St-II primary structure confirms the partial revision of cytolysin III amino acid sequence. All nonconservative changes between St-I and St-II are located at the N-terminal. According to our prediction these changes could be located at the same face of an alpha-helix during pore formation events and could account for the observed differences in hemolytic activity between St-I and St-II.
authors: Physical-Chemistry Division, Protein Structure Department, Center for Genetic Engineering and Biotechnology, P.O. Box 6162, Havana City, Cuba.
authors: V
authors: V
authors: Huerta
authors: V
authors: V
authors: Morera
authors: Y
authors: Y
authors: Guanche
authors: G
authors: G
authors: Chinea
authors: L J
authors: LJ
authors: González
authors: L
authors: L
authors: Betancourt
authors: D
authors: D
authors: Martínez
authors: C
authors: C
authors: Alvarez
authors: M E
authors: ME
authors: Lanio
authors: V
authors: V
authors: Besada
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003064:Cnidarian Venoms / Q000737:chemistry* / Q000633:toxicity; D006460:Hemolysin Proteins / Q000737:chemistry* / Q000633:toxicity; D006461:Hemolysis / Q000187:drug effects*; D008969:Molecular Sequence Data; D009930:Organic Chemicals; D017433:Protein Structure, Secondary
chemical_list: D003064:Cnidarian Venoms; D006460:Hemolysin Proteins; D009930:Organic Chemicals; C404794:sticholysin II; C121348:stycholysin I