STRUCTURE DETERMINATION OF FERRIC ENTEROBACTIN RECEPTOR FROM E COLI

铁结肠素受体(Fepa)是一种大肠杆菌的外膜 一种蛋白质，其功能是寻找一种铁-螯合剂络合物，铁 肠毒素，并将其通过外膜运输。费帕是一位 一类外膜转运体的成员，它识别 它们的底物具有高特异性和催化活性转运 穿过外膜。不存在此成员的任何结构 运输机的等级。因为这种蛋白质不含游离 半胱氨酸，5个半胱氨酸突变体已通过定点创建 用重原子辅助衍生化的诱变。

Ferric enterobactin receptor (FepA) is an E. coli outer membrane protein which functions to find an iron-chelator complex, ferric enterobactin, and transport it through the outer membrane. FepA is a member of a class of outer membrane transporters which recognizes their substrates with high specificity and catalyze active transport across the outer membrane. No structure exists for any member of this class of transporters. Because the protein contains no free cysteines, five cysteine mutants have been created by site-directed mutagenesis to aid derivatization with heavy atoms.