Bipartite tetracysteine display requires site flexibility for ReAsH coordination

Chembiochem. 2009 Jul 6;10(10):1644-7. doi: 10.1002/cbic.200900207.

Abstract

Flexibility required: We designed intramolecular bipartite tetracysteine sites in loops of p53 and the beta-sheets of EmGFP. We found that ReAsH binding preferentially favors tetracysteine sites with flexible geometries such as loops; flexibility was assessed by comparing Calpha B-factor values. This information is important for directing successful bipartite tetracysteine site designs.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Arsenicals / chemistry*
  • Binding Sites
  • Cysteine / chemistry*
  • Fluorescent Dyes / chemistry
  • Green Fluorescent Proteins / chemistry
  • Oxazines / chemistry*
  • Protein Binding
  • Protein Folding
  • Protein Structure, Tertiary
  • Tumor Suppressor Protein p53 / chemistry

Substances

  • Arsenicals
  • Fluorescent Dyes
  • Oxazines
  • ReAsH-EDT2 compound
  • Tumor Suppressor Protein p53
  • Green Fluorescent Proteins
  • Cysteine