Fig. 9: Schematic showing a structure-based mechanism of FBI-GS activation of GlnR proteins in Gram-positive bacteria. | Nature Communications

Fig. 9: Schematic showing a structure-based mechanism of FBI-GS activation of GlnR proteins in Gram-positive bacteria.

From: Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria

Fig. 9

GS and GlnR are shown as schematic surface renderings with GS subunits colored gray and green and GlnR subunits colored pink and light blue. In the model GlnR binding stabilizes or facilitates subunit exchange and, in some bacteria, the transition of GS from a dodecamer to a tetradecamer. GlnR is monomeric but the interaction of two GlnR subunits in the same side pore brings them into proximity and allows them to dimerize on cognate DNA (shown as a yellow cartoon) and thus regulate genes important in nitrogen homeostasis.

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