Structural characterization of Myxococcus xanthus MglC, a component of polarity control system, and its interactions with MglB
Myxococcus xanthus displays two types of motilities i.e. Social (S) and Adventurous (A). The pole-to-pole reversals of these motility regulator proteins is the key to this process. Here, we determined ~1.85 [A] resolution crystal structure of MglC, which revealed that despite sharing <9% sequence identity, both MglB and MglC adopt Regulatory Light Chain 7 (RLC7) family fold. Interestingly, MglC is structurally unique compared to the other known RLC7 family proteins having ~30{degrees}-40{degrees} shift in the orientation of functionally important 2 helix. Using isothermal titration calorimetry and gel filtration chromatography, we show that MglC binds MglB in 2:4 stoichiometry with submicromolar range dissociation constant. Using combination of small angle X-ray scattering and molecular docking studies, we show that MglBC complex is formed by MglC homodimer sandwiched between two homodimers of MglB. In BriefKapoor et al. report the crystal structure of Myxococcus xanthus MglC, a Roadblock Light Chain 7 (RLC7) family protein, involved in polarity reversal. The structure reveals a distinct orientation of 2 helix compared to other RLC7 proteins. They also demonstrate that MglC binds a GTPase activating protein, MglB, with submicromolar range dissociation constant. HighlightsO_LIMglC adopts RLC7 fold and has distinct structural features. C_LIO_LIMglC interacts MglB to form a stable complex having submicromolar range dissociation constant. C_LIO_LIMglC homodimer is sandwiched between two MglB homodimers to form a 2:4 stoichiometric complex. C_LI