Allosteric regulation of a prokaryotic small Ras-like GTPase contributes to cell polarity oscillations in bacterial motility
Fig 6
Conservation of sequence features of the allosteric pocket on MglA and MglB Ct-helix.
(A) Comparison of residue conservation in C-terminal extension of coupled versus orphan MglB sequences. The aspartate residues implicated in interaction with the allosteric pocket on MglA are highlighted by “*” in the sequence conservation logo. The fractional occupancy of amino acids in the sequence alignment is shown for each amino acid position. The numbers within brackets denote the number of sequences in the alignment. The residues are colored in 20 different shades. (B) Comparison of residue conservation in the α5 helix of MglA sequences coupled with MglB sequences possessing a negatively charged C-terminal extension versus that of all coupled MglA sequences. The lysine residues that potentially interact with the Ct-helix of MglB are highlighted by “*” in the sequence conservation logo. The fractional occupancy of amino acids in the sequence alignment is shown for each amino acid position. The numbers within brackets denote the number of sequences in the alignment. Ct-helix, C-terminal helix; MglA, Mutual Gliding motility A; MglB, Mutual Gliding motility B.