FIGURE 1.
The Cbz-LPAT* modifier and NMR data of its complex with SrtAΔN59. a, chemical structure of the Cbz-LPAT* peptide analog. b, comparison of the chemical structure of the thioacyl enzyme-substrate intermediate of the anchoring reaction (top) and the disulfide-linked covalent complex between the Cbz-LPAT* peptide and Cys184 of SrtAΔN59 (bottom). c, selected panels showing intermolecular NOEs between the SrtAΔN59 protein and the sorting signal peptide. The panels are taken from a three-dimensional (F1) 13C, 15N-filtered, (F2) 13C-edited NOESY-HSQC spectrum of the SrtAΔN59-LPAT* complex dissolved in 2H2O. The identity of the proton from SrtAΔN59 and its chemical shift are shown at the top and bottom of each panel, respectively. On the right side of each cross-peak the sorting signal peptide proton that is proximal to the protein is indicated.