Fig. 6: Synthase activation and polymer modifications in β- and γ-Proteobacteria. | Nature Communications

Fig. 6: Synthase activation and polymer modifications in β- and γ-Proteobacteria.

From: Structural basis for synthase activation and cellulose modification in the E. coli Type II Bcs secretion system

Fig. 6

In addition to direct c-di-GMP complexation at micromolar dinucleotide concentrations, BcsA can be activated or stabilized in a catalytically competent conformation by a high-affinity c-di-GMP-sensing BcsRQEF cytosolic vestibule complex or by macromolecular intracellular scaffolds. In the periplasm, the polymer can undergo chemical modifications by the pEtN-transferase BcsG or by a multicomponent Wss cellulose acetylation complex. Finally, the polymer can undergo limited hydrolysis by the periplasmic endoglucanase BcsZ. OM outer membrane, PG peptidoglycan, IM inner membrane.

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