1H, 13C, and 15N NMR assignments of StnII-Y111N, a highly impaired mutant of the sea anemone actinoporin Sticholysin II

Biomol NMR Assign. 2010 Apr;4(1):69-72. doi: 10.1007/s12104-010-9214-0. Epub 2010 Feb 18.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carbon Isotopes / chemistry
  • Cnidarian Venoms / chemistry*
  • Cnidarian Venoms / genetics*
  • Escherichia coli
  • Genetic Variation
  • Hydrogen / chemistry
  • Hydrogen-Ion Concentration
  • Mutant Proteins / chemistry
  • Mutation, Missense*
  • Nitrogen Isotopes / chemistry
  • Nuclear Magnetic Resonance, Biomolecular
  • Sea Anemones / chemistry*
  • Temperature

Substances

  • Carbon Isotopes
  • Cnidarian Venoms
  • Mutant Proteins
  • Nitrogen Isotopes
  • sticholysin II
  • Hydrogen