6YBU

Crystal structure of a native BcsE (349-523) RQ complex with c-di-GMP and ATP bound

Summary for 6YBU

• Entry DOI: 10.2210/pdb6ybu/pdb
• Related: 6TJ0 6YAR 6YAY 6YB3 6YB5 6YBB 6YG8
• Descriptor: Bacterial cellulose secretion regulator BcsQ, Bacterial cellulose secretion regulator BcsR, Bacterial cellulose secretion regulator BcsE, residues 349-523, ... (7 entities in total)
• Functional Keywords: bacterial biofilms, bacterial cellulose, bacterial secretion system, atp binding protein, c-di-gmp binding protein, signaling protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 12
• Total formula weight: 230424.27

Authors

Abidi, W.,Zouhir, S.,Roche, S.,Krasteva, P.V. (deposition date: 2020-03-17, release date: 2021-02-24, Last modification date: 2024-01-24)

Primary citation

Abidi, W.,Zouhir, S.,Caleechurn, M.,Roche, S.,Krasteva, P.V.
Architecture and regulation of an enterobacterial cellulose secretion system.
Sci Adv, 7:-, 2021

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

Experimental method

X-RAY DIFFRACTION (2.49 Å)