1H, 13C, and 15N NMR assignments of StnII-Y111N, a highly impaired mutant of the sea anemone actinoporin Sticholysin II.
Sticholysin II is an actinoporin of 175 amino acids produced by the sea anemone Stichodactyla helianthus. Several studies with different mutants have been performed to characterize its molecular properties and activity. As a first step towards a 3D structural characterization and its interaction with membrane models at a residue level, herein we report the nearly complete NMR (15)N, (13)C and (1)H chemical shifts assignments of the Y111N variant at pH 4.0 and 25 degrees C (BMRB No. 16630). The assignment is complete for the biologically relevant residues, specially for those implicated in membrane interactions.
Pardo-Cea
Miguel A
MA
Departamento de Espectroscopía y Estructura Molecular, Instituto de Química Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.
Alegre-Cebollada
Jorge
J
Martínez-del-Pozo
Alvaro
A
Gavilanes
José G
JG
Bruix
Marta
M
D000595:Amino Acid Sequence; D000818:Animals; D002247:Carbon Isotopes / Q000737:chemistry; D003064:Cnidarian Venoms / Q000737:chemistry* / Q000235:genetics*; D004926:Escherichia coli; D014644:Genetic Variation; D006859:Hydrogen / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D050505:Mutant Proteins / Q000737:chemistry; D020125:Mutation, Missense; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D012615:Sea Anemones / Q000737:chemistry*; D013696:Temperature
D002247:Carbon Isotopes; D003064:Cnidarian Venoms; D050505:Mutant Proteins; D009587:Nitrogen Isotopes; C404794:sticholysin II; D006859:Hydrogen