6yb5
Orthorhombic crystal structure of a native BcsRQ complex crystallized in the presence of ADP
Structural highlights
FunctionBCSQ_ECOLI Essential for cellulose biosynthesis, shown for strain 1094, a commensal, natural cellulose producer (PubMed:19400787). Also shown in strain W3110 which has a restored reading frame (TAG stop codon to TTG for amino acid 6, called strain AR3110), this protein (PubMed:24097954). May play a role in subcellular localization of an active cellulose biosynthesis apparatus at the bacterial cell pole (PubMed:19400787). The combination of cellulose and the curli fiber network confer cohesion, elasticity and tissue-like properties to colonies (PubMed:24097954).[1] [2] Publication Abstract from PubMedMany free-living and pathogenic enterobacteria secrete biofilm-promoting cellulose using a multicomponent, envelope-embedded Bcs secretion system under the control of intracellular second messenger c-di-GMP. The molecular understanding of system assembly and cellulose secretion has been largely limited to the crystallographic studies of a distantly homologous BcsAB synthase tandem and a low-resolution reconstruction of an assembled macrocomplex that encompasses most of the inner membrane and cytosolic subunits and features an atypical layered architecture. Here, we present cryo-EM structures of the assembled Bcs macrocomplex, as well as multiple crystallographic snapshots of regulatory Bcs subcomplexes. The structural and functional data uncover the mechanism of asymmetric secretion system assembly and periplasmic crown polymerization and reveal unexpected subunit stoichiometry, multisite c-di-GMP recognition, and ATP-dependent regulation. Architecture and regulation of an enterobacterial cellulose secretion system.,Abidi W, Zouhir S, Caleechurn M, Roche S, Krasteva PV Sci Adv. 2021 Jan 27;7(5). pii: 7/5/eabd8049. doi: 10.1126/sciadv.abd8049. Print , 2021 Jan. PMID:33563593[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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