Fig. 3: Negatively-charged residues on the putative C-terminal tail helix of MlaA are important for MlaC recruitment. | Nature Communications

Fig. 3: Negatively-charged residues on the putative C-terminal tail helix of MlaA are important for MlaC recruitment.

From: Molecular mechanism of phospholipid transport at the bacterial outer membrane interface

Fig. 3

a Cartoon representation of the EcMlaA (teal) model generated from AlphaFold2 (AF-P76506-F1)35 with the putative C-terminal tail helix colored blue. C-terminal truncation positions (CTDs) are annotated. MlaC-crosslinking residue Q205 is labeled in orange sticks. Charge-reversed residues in MlaA2DD2R and MlaA2DE2R are labeled in red and pink sticks respectively. b Representative immunoblots showing abolishment of disulfide crosslinks between MlaA and MlaC in ΔmlaA ΔmlaC cells expressing various C-terminal tail helix mutants of MlaAQ205C(-His) and MlaCV171C-His from the pCDF and pET22/42 plasmids, respectively. Samples were subjected to non-reducing (left) or reducing (right) SDS-PAGE prior to immunoblotting. The experiment had been performed at least three times with similar results. Source data are provided as a Source Data file.

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