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6YG8

Cryo-EM structure of a BcsB pentamer in the context of an assembled Bcs macrocomplex

Summary for 6YG8
Entry DOI10.2210/pdb6yg8/pdb
Related6TJ0 6YAR 6YAY 6YB3 6YB5 6YBB 6YBU
EMDB information10799 11356 11836
DescriptorBacterial cellulose secretion regulator BcsB (1 entity in total)
Functional Keywordsbacterial biofilms, bacterial cellulose, bacterial secretion system, regulator protein, signaling protein
Biological sourceEscherichia coli
Total number of polymer chains5
Total formula weight430921.92
Authors
Zouhir, S.,Krasteva, P.V. (deposition date: 2020-03-27, release date: 2021-02-24)
Primary citationAbidi, W.,Zouhir, S.,Caleechurn, M.,Roche, S.,Krasteva, P.V.
Architecture and regulation of an enterobacterial cellulose secretion system.
Sci Adv, 7:-, 2021
Cited by
PubMed Abstract: 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.
PubMed: 33563593
DOI: 10.1126/sciadv.abd8049
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3 Å)
Structure validation

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