Structural and Functional Characterization of the BcsG Subunit of the Cellulose Synthase in Salmonella typhimurium.

Sun L, Vella P, Schnell R, Polyakova A, Bourenkov G, Li F, Cimdins A, Schneider TR, Lindqvist Y, Galperin MY, Schneider G, Römling U

J. Mol. Biol. 430 (18 Pt B) 3170-3189 [2018-09-14; online 2018-07-12]

Many bacteria secrete cellulose, which forms the structural basis for bacterial multicellular aggregates, termed biofilms. The cellulose synthase complex of Salmonella typhimurium consists of the catalytic subunits BcsA and BcsB and several auxiliary subunits that are encoded by two divergently transcribed operons, bcsRQABZC and bcsEFG. Expression of the bcsEFG operon is required for full-scale cellulose production, but the functions of its products are not fully understood. This work aimed to characterize the BcsG subunit of the cellulose synthase, which consists of an N-terminal transmembrane fragment and a C-terminal domain in the periplasm. Deletion of the bcsG gene substantially decreased the total amount of BcsA and cellulose production. BcsA levels were partially restored by the expression of the transmembrane segment, whereas restoration of cellulose production required the presence of the C-terminal periplasmic domain and its characteristic metal-binding residues. The high-resolution crystal structure of the periplasmic domain characterized BcsG as a member of the alkaline phosphatase/sulfatase superfamily of metalloenzymes, containing a conserved Zn

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PubMed 30017920

DOI 10.1016/j.jmb.2018.07.008

Crossref 10.1016/j.jmb.2018.07.008

S0022-2836(18)30758-7

PDB 5OJH [Crystal structure of the extramembrane domain of the cellulose biosynthetic protein BcsG from Salmonella typhimurium]

PDB 5OLT [Crystal structure of the extramembrane domain of the cellulose biosynthetic protein BcsG from Salmonella typhimurium]