6ybb | pdb_00006ybb

Crystal structure of a native BcsE (217-523) - BcsR-BcsQ (R156E mutant) complex with c-di-GMP and ATP bound

spinqualitylabelsall models 6ybb, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ybb is a 6 chain structure with sequence from Escherichia coli and Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: ATP, C2E, GOL, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BCSQ_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). Publication Abstract from PubMed Many 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA