9NQD
Structure of Pseudomonas FapC Biofilm-Forming Functional Amyloid
This is a non-PDB format compatible entry.
Summary for 9NQD
Entry DOI | 10.2210/pdb9nqd/pdb |
EMDB information | 49649 |
Descriptor | Functional amyloid subunit FapC (1 entity in total) |
Functional Keywords | fapc functional amyloid pseudomonas c, amyloid, fibril, biofilm, functional amyloid, structural protein |
Biological source | Pseudomonas fluorescens |
Total number of polymer chains | 12 |
Total formula weight | 270890.81 |
Authors | Hansen, K.H.,Golcuk, M.,Byeon, C.B.,Plechinger, E.B.,Conway, J.F.,Andreasen, M.,Gur, M.,Akbey, U. (deposition date: 2025-03-12, release date: 2025-06-25, Last modification date: 2025-10-08) |
Primary citation | Hansen, K.H.,Golcuk, M.,Byeon, C.H.,Tunc, A.,Plechinger, E.B.,Dueholm, M.K.D.,Conway, J.F.,Andreasen, M.,Gur, M.,Akbey, U. Structural basis of Pseudomonas biofilm-forming functional amyloid FapC formation. Sci Adv, 11:eadx7829-eadx7829, 2025 Cited by PubMed Abstract: Biofilm-protected causes chronic infections that are difficult to treat. FapC, the major biofilm-forming functional amyloid in , is essential for biofilm integrity, yet its structural details remain unresolved. Using an integrative structural biology approach, we combine a solution nuclear magnetic resonance-based structural ensemble of unfolded monomeric FapC, a ~3.3-angstrom-resolution cryo-electron microscopy (cryo-EM) density map of FapC fibril, and all-atom molecular dynamics (MD) simulations to capture the transition from the unfolded to folded monomer to the fibrillar fold, providing a complete structural view of FapC biogenesis. Cryo-EM reveals a unique irregular triple-layer β solenoid cross-β fibril composed of a single protofilament. MD simulations initiated from monomeric and fibrillar FapC mapped structural transitions, offering mechanistic insights into amyloid assembly and disassembly. Understanding FapC reveals how exploits functional amyloids for biofilm formation, and establishes a structural and mechanistic foundation for developing therapeutics targeting biofilm-related infection and antimicrobial resistance. PubMed: 40991694DOI: 10.1126/sciadv.adx7829 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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