Fig. 2: Structural model for the cytoplasmic ATPase ring complex. | Communications Biology

Fig. 2: Structural model for the cytoplasmic ATPase ring complex.

From: A positive charge region of Salmonella FliI is required for ATPase formation and efficient flagellar protein export

Fig. 2

a Cα ribbon representation of the FliH2FliI complex (PDB ID: 5B0O). Arg-26 (R26), Arg-27 (R27), Arg-30 (R30), Arg-33 (R33), Arg-76 (R76), and Arg-93 (R93) form a positive charge cluster on the molecular surface of the N-terminal domain of FliI. The C-terminal domain of FliH forms a dimer (FliHC2) to bind to the N-terminal α-helix consisting of residues 2–21 of FliI and the positive charge cluster. Arg-33 and Arg-76 are located at an interface between FliI subunits, and Arg-76 is in very close proximity of Asn-73 (N73) of its nearest FliI subunit. b Multiple sequence alignment of the N-terminal domain of FliI orthologs. Multiple sequence alignment was carried out by Clustal Omega. Conserved residues are labeled with blue colors. UniProt Accession numbers: Salmonella, P26465; Vibrio, A0A1Q1PM95; Caulobacter, B8H363; Helicobacter, O07025, Thermotoga, A0A2N5RHQ8; Bacillus, P23445.

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