6SI7
Structure of the curli secretion-assembly complex CsgG:CsgF
Summary for 6SI7
| Entry DOI | 10.2210/pdb6si7/pdb |
| EMDB information | 10206 |
| Descriptor | Curli production assembly/transport component CsgF, Curli production assembly/transport component CsgG (2 entities in total) |
| Functional Keywords | secretion channel, curli, outer membrane protein, nanopore sensing, protein transport, bacterial amyloid |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 18 |
| Total formula weight | 394695.45 |
| Authors | Van der Verren, S.E.,Remaut, H. (deposition date: 2019-08-08, release date: 2020-06-24, Last modification date: 2024-05-22) |
| Primary citation | Van der Verren, S.E.,Van Gerven, N.,Jonckheere, W.,Hambley, R.,Singh, P.,Kilgour, J.,Jordan, M.,Wallace, E.J.,Jayasinghe, L.,Remaut, H. A dual-constriction biological nanopore resolves homonucleotide sequences with high fidelity. Nat.Biotechnol., 38:1415-1420, 2020 Cited by PubMed Abstract: Single-molecule long-read DNA sequencing with biological nanopores is fast and high-throughput but suffers reduced accuracy in homonucleotide stretches. We now combine the CsgG nanopore with the 35-residue N-terminal region of its extracellular interaction partner CsgF to produce a dual-constriction pore with improved signal and base-calling accuracy for homopolymer regions. The electron cryo-microscopy structure of CsgG in complex with full-length CsgF shows that the 33 N-terminal residues of CsgF bind inside the β-barrel of the pore, forming a defined second constriction. In complexes of CsgG bound to a 35-residue CsgF constriction peptide, the second constriction is separated from the primary constriction by ~25 Å. We find that both constrictions contribute to electrical signal modulation during single-stranded DNA translocation. DNA sequencing using a prototype CsgG-CsgF protein pore with two constrictions improved single-read accuracy by 25 to 70% in homopolymers up to 9 nucleotides long. PubMed: 32632300DOI: 10.1038/s41587-020-0570-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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