Fig. 6: Model of cellulose pEtN modification and secretion. | Nature Communications

Fig. 6: Model of cellulose pEtN modification and secretion.

From: Insights into phosphoethanolamine cellulose synthesis and secretion across the Gram-negative cell envelope

Fig. 6

BcsA recruits three copies of BcsG to the cellulose biosynthesis site via its N-terminal cytosolic domain. The catalytic domain of BcsG either faces the lipid bilayer to receive a pEtN group or contacts the nascent cellulose chain for modification. BcsC interacts with the terminal BcsB subunit of the semicircle to establish an envelope-spanning complex. Cellulose is guided towards the OM through interactions with the TPR solenoid. BcsZ may degrade cellulose to prevent stalling of the biosynthetic machinery or mislocalization of cellulose to the periplasm. The cytosolic BcsE and BcsQR as well as BcsF components are omitted for clarity. PE phosphatidylethanolamine lipid, DAG diacylglycerol, pEtN phosphoethanolamine, IM, and OM inner and outer membrane, respectively.

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