Fig. 5: The synthase macrocomplex in limiting c-di-GMP. | Nature Communications

Fig. 5: The synthase macrocomplex in limiting c-di-GMP.

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

Fig. 5

a Locally refined cryo-EM map and fitted structure of the crownless synthase macrocomplex featuring a c-di-GMP-free synthase in two different views. IM inner membrane. b Cartoon representation of the same assembly. c The cryo-EM map and model of a locally refined BcsRQEF assembly. d A zoom-in on c-di-GMP binding by a composite, dual I-site pocket in closed BcsE. e REC* domain dimerization interface in the non-saturated macrocomplex. f A zoom-in on the BcsA:BcsR interface and summary of the synthase’s interactions with the cytosolic vestibule partners57. g Overall core synthase fold showing unstructured gating loop and an accessible active site.

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