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. 2022 Feb 23;13:1022. doi: 10.1038/s41467-022-28361-1

Fig. 2. LtaA adopts inward- and outward-facing states.

Fig. 2

Selected residues for cross-linking of LtaA in inward-facing conformation (a) and outward-facing conformation (b). N-terminal and C-terminal domains are shown in light orange and light blue, respectively. The relative abundance of cysteine-containing peptides in absence (−) or presence (+) of N,N’-(o-phenylene)-dimaleimide (o-PDM) is shown in histograms. Collision-induced dissociation (CID) spectrum of cysteine-containing peptides and elution profiles of peptide fragments are shown in Supplementary Fig. 3. Error bars indicate + /− standard deviation (s.d.) (n = 3, biological replicates). *P ≤ 0.05, **P ≤ 0.01, ***P ≤ 0.001, ****P ≤ 0.0001. Asterisks mark the result from unpaired t test. c Cross-linking analysis of LtaA in proteoliposomes. Positions of selected cysteine pairs at the extracellular and cytoplasmic regions of LtaA are shown as spheres. SDS-PAGE show band shifts of samples treated with mPEG5K after irreversible cross-link with o-PDM. Separated species are indicated with arrows. The complete gel is shown in Supplementary Fig. 4C. SDS-PAGE experiments were independently repeated at least three times with similar results. Source data are provided as a Source Data file.