title: Bipartite tetracysteine display requires site flexibility for ReAsH coordination.
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.
authors.affiliation: Department of Chemistry, Yale University, 275 Prospect Street, New Haven, CT 06511, USA.
authors.forename: Jessica L
authors.initials: JL
authors.lastname: Goodman
authors.forename: Daniel B
authors.initials: DB
authors.lastname: Fried
authors.forename: Alanna
authors.initials: A
authors.lastname: Schepartz
mesh_terms: 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
chemical_list: D001152:Arsenicals; D005456:Fluorescent Dyes; D010078:Oxazines; C454115:ReAsH-EDT2 compound; D016159:Tumor Suppressor Protein p53; D049452:Green Fluorescent Proteins; D003545:Cysteine