Extended Data Fig. 1: Protein purification and ATPase activity characterization.
From: An oligopeptide permease, OppABCD, requires an iron–sulfur cluster domain for functionality
a, Size exclusion chromatography of OppABCD, OppAW491ABCD, OppABCDE-D and OppA53-591aa samples, respectively. SDS-PAGE analysis results are also shown. b, ATPase activity of OppABCD plotted against varying ATP concentrations. c, ATPase activities of wild-type OppABCD (WT), OppAW491ABCD (APO) and OppABCDE-D (E2D). d, e, ATPase activities of OppABCD and OppAW491ABCD, respectively, in the presence of 2 mM GSH, Tri-DAP, GE81112, bradykinin, synthesized octapeptide (SLKVSVDP), synthesized nonapeptide-1 (ASPFSPDPP), nonapeptide-2 (ALPVSTDPA) and nonapeptide-3 (ALPVSVDPA). The ATPase rates in d and e are normalized based on the values of OppABCD ( ~ 200 nmol mg-1 min-1) and OppAW491ABCD (~65 nmol mg-1 min-1), respectively. In b-e, error bars represent mean ± SD based on three independent measurements. f, Heat map of ATPase activities of OppABCD and OppAW491ABCD in the presence of peptides with different lengths. Uncropped images for panel a are available as Source Data. Statistics for panels b-f are available as Source Data.
