Fig. 7: GlnR–DNA structures. | Nature Communications

Fig. 7: GlnR–DNA structures.

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

Fig. 7: GlnR–DNA structures.The alternative text for this image may have been generated using AI.

A Multiple sequence alignment of the Bs, Sa, Lm, and Pp GlnR proteins with secondary structural elements (from Bs, Sa, and Lm) shown above the alignments. Residues in the N-terminal domains are highlighted in yellow, those in the wHTH are in pink and those in the C-terminal region are green. C-tail residues that bind FBI-GS are highlighted in red. Residues not observed in either the GlnR–DNA or FBI-GS-GlnR structures are not highlighted and form the flexible linker connecting domains. Secondary structural elements are indicated over the sequence alignments. B Structure of the Sa GlnR–DNA complex, with one subunit colored as in A and the other colored gray. C Superimpositions of the Sa, Bs, and Lm GlnR–DNA complexes, which are colored slate, salmon and cyan, respectively. D Electrostatic surface diagrams of Sa, Bs, and Lm GlnR proteins bound to DNA. Blue and red represent electropositive and electronegative surfaces, respectively. The figure was generated as a charged smoothed potential in PyMOL (Sa GlnR-DNA charge potentials levels range from −86 to +86, Bs GlnR-DNA from −73.7 to +73.7, and the Lm GlnR-DNA from −81.3 to +81.3).

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