Fig. 1: MlaA contacts MlaC in cells via C-terminal α-helices at the periplasmic opening of its hydrophilic channel. | Nature Communications

Fig. 1: MlaA contacts MlaC in cells via C-terminal α-helices at the periplasmic opening of its hydrophilic channel.

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

Fig. 1

a Representative immunoblots showing UV-dependent formation of strong crosslinks between MlaA and MlaC in ΔmlaA cells expressing MlaA-His substituted with pBpa at indicated positions from the pCDF plasmid. Additional but unidentified MlaApBpa-His crosslinked adducts were detected and denoted with an asterisk (*). The experiment had been performed at least three times with similar results. Source data are provided as a Source Data file. b Membrane (left) and periplasmic (right) views of cartoon representations of the crystal structure of Klebsiella pneumoniae OmpK36 (green)-MlaA (cyan) (PDB: 5NUP)32 with positions (EcMlaA numbering) that crosslink to MlaC highlighted. Residues exhibiting strong, weak, or no photo-crosslinks with MlaC are illustrated in red and pink sticks, or in gray respectively (see Supplementary Table 4). The OM boundaries are indicated as gray dashed lines.

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