9QOG

Crystal structure of Nanofitin C10 in complex with a a double-helical aromatic oligoamide foldamer

This is a non-PDB format compatible entry.

Summary for 9QOG

• Entry DOI: 10.2210/pdb9qog/pdb
• Descriptor: Nanofitin C10, Aromatic oligoamide foldamer, SULFATE ION, ... (6 entities in total)
• Functional Keywords: protein-foldamer complex, affitin, nanofitin, symmetry assembly, aof, aromatic oligoamide foldamer, homo-double helix, de novo protein
• Biological source: Sulfolobus acidocaldarius (human); More
• Total number of polymer chains: 4
• Total formula weight: 20183.83

Authors

Sigl, J.C.,Sachs, J.,Merlet, E.,Ferrand, Y.,Huc, I. (deposition date: 2025-03-26, release date: 2026-04-08, Last modification date: 2026-08-26)

Primary citation

Sigl, J.,Morozov, V.,Wang, L.,Sachs, J.,Merlet, E.,Largy, E.,Geue, N.,Osterlund, N.,Kwon, S.,Sanchez, F.,Candela, L.,Huet, S.,Pagel, K.,Ferrand, Y.,Douat, C.,Mackereth, C.D.,Huc, I.
A protein-foldamer supramolecular synthon for self-assembled hybrid architectures.
Nat.Chem., 2026

PubMed Abstract: Constructing artificial assemblies that combine proteins and synthetic ligands has been hampered by the lack of protein-ligand interfaces that are sufficiently large and organized to enable precise structural control. Here ribosome display selection is used to identify a protein that binds a helical aromatic foldamer both tightly and selectively through a sizeable surface area. We used this complex as a supramolecular synthon to create well-defined hybrid foldamer-protein architectures. Examples include foldamers that bind two proteins and hold them at a precise distance, proteins that bind two foldamers and crystals in which proteins and foldamers are connected in cyclic or infinite arrays. The modularity of aromatic foldamers brings a further dimension to protein-based assemblies.

PubMed: 42608459
DOI: 10.1038/s41557-026-02222-6

Experimental method

X-RAY DIFFRACTION (1.85 Å)