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. Author manuscript; available in PMC: 2009 Oct 9.
Published in final edited form as: Mol Microbiol. 2008 Dec;70(5):1223–1235. doi: 10.1111/j.1365-2958.2008.06477.x

Fig. 3. Structure of S. meliloti LsrB and its ligand.

Fig. 3

A. Ribbon diagram of SmLsrB. The ribbon diagram is colored in rainbow order from N- to C- terminus. The bound ligand and the corresponding electron density are shown.

B. Stereoview of 2Fo-Fc ligand electron density. The DPD isomer R-THMF is shown modeled into non-protein electron density in the receptor binding site.

C. Comparison of the of the S. meliloti and S. typhimurium LsrB AI-2 binding sites. Overlay of the SmLsrB (green) and S. typhimurium LsrB (yellow) binding sites based on overall alignment of the protein structures as calculated by PyMOL. Residue numbers are from the S. meliloti sequence. Dashed red lines indicate potential hydrogen bonds and the interacting residues are labeled in red.