Extended Data Fig. 5: Structural details of second messenger binding to SmbA. | Nature Microbiology

Extended Data Fig. 5: Structural details of second messenger binding to SmbA.

From: Reciprocal growth control by competitive binding of nucleotide second messengers to a metabolic switch in Caulobacter crescentus

Extended Data Fig. 5

(a) Cartoon representation of the (c-di-GMP)2 complex with full structural details of the ligands and interacting residues. H-bonds (length < 3.5 Å) and cation - π interactions are indicated by red and magenta lines, respectively. Note that R133*, which forms lateral H-bonds with O6 and N7 of g2 and cation - π interaction with g1, is donated by an adjacent protomer in the crystal packing (see Supplementary Fig. 7a). (b) Structure of the ppGpp complex. Note that the C-terminal carboxylate of a symmetry related protomer is forming a salt-bridge with R251 (see Supplementary Fig. 7b). (c) 2Fo-Fc omit maps contoured at 1.2 σ of (c-di-GMP)2 (left) and ppGpp (right) as bound to SmbA. (d) Fo-Fc omit maps contoured at 3.0 σ of (c-di-GMP)2 (left) and ppGpp (right).

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