6L7C

CsgFG complex with substrate CsgAN6 peptide in Curli biogenesis system

Summary for 6L7C

• Entry DOI: 10.2210/pdb6l7c/pdb
• EMDB information: 0842
• Descriptor: Curli production assembly/transport protein CsgG, CsgF, Major curlin subunit CsgA (3 entities in total)
• Functional Keywords: biofilm, curli biogenesis system, csgfg complex, substrate csga, protein transport
• Biological source: Escherichia coli O69:H11 str. 08-4661; More
• Total number of polymer chains: 27
• Total formula weight: 428433.33

Authors

Yan, Z.F.,Yin, M.,Chen, J.N.,Li, X.M. (deposition date: 2019-11-01, release date: 2020-01-15, Last modification date: 2024-03-27)

Primary citation

Yan, Z.,Yin, M.,Chen, J.,Li, X.
Assembly and substrate recognition of curli biogenesis system.
Nat Commun, 11:241-241, 2020

PubMed Abstract: A major component of bacterial biofilms is curli amyloid fibrils secreted by the curli biogenesis system. Understanding the curli biogenesis mechanism is critical for developing therapeutic agents for biofilm-related infections. Here we report a systematic study of the curli biogenesis system, highlighted by structural, biochemical and functional analysis of the secretion channel complexes (CsgF-CsgG) with and without the curli substrate. The dual-pore architecture of the CsgF-CsgG complex was observed and used to develop an approach to inhibit the curli secretion by physically reducing the size of the CsgF pore. We further elucidated the assembly of the CsgFG complex with curli components (CsgA and CsgB) and curli-cell association through CsgF. Importantly, the recognition of the CsgA substrate by CsgG was uncovered. Nine crevices outside of the CsgG channel provide specific and highly-conserved recognition sites for CsgA N-terminus. Together with analysis of CsgE, our study provides comprehensive insights into curli biogenesis.

PubMed: 31932609
DOI: 10.1038/s41467-019-14145-7

Experimental method

ELECTRON MICROSCOPY (3.34 Å)