Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2020.08.27.270058v1?rss=1 Authors: Kapoor, S., Kodesia, A., Kalidas, N., Ganguly, A., Thakur, K. G. Abstract: 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 angstrom 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{ring}-40{ring} 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. Copy rights belong to original authors. Visit the link for more info