Bipartite tetracysteine display requires site flexibility for ReAsH coordination.
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.
Goodman
Jessica L
JL
Department of Chemistry, Yale University, 275 Prospect Street, New Haven, CT 06511, USA.
Fried
Daniel B
DB
Schepartz
Alanna
A
D000595:Amino Acid Sequence; D001152:Arsenicals / Q000737:chemistry*; D001665:Binding Sites; D003545:Cysteine / Q000737:chemistry*; D005456:Fluorescent Dyes / Q000737:chemistry; D049452:Green Fluorescent Proteins / Q000737:chemistry; D010078:Oxazines / Q000737:chemistry*; D011485:Protein Binding; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry
D001152:Arsenicals; D005456:Fluorescent Dyes; D010078:Oxazines; C454115:ReAsH-EDT2 compound; D016159:Tumor Suppressor Protein p53; D049452:Green Fluorescent Proteins; D003545:Cysteine