9ATW
Structure of biofilm-forming functional amyloid PSMa1 from Staphylococcus aureus
This is a non-PDB format compatible entry.
Summary for 9ATW
| Entry DOI | 10.2210/pdb9atw/pdb |
| EMDB information | 43835 |
| Descriptor | Phenol-soluble modulin alpha 1 peptide (1 entity in total) |
| Functional Keywords | functional amyloid fibril, biofilm, bacterial biofilm, phenol soluble modulin alpha1, psma1, structural protein |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 64 |
| Total formula weight | 144820.29 |
| Authors | Hansen, K.H.,Byeon, C.H.,Liu, Q.,Drace, T.,Boesen, T.,Conway, J.F.,Andreasen, M.,Akbey, U. (deposition date: 2024-02-27, release date: 2024-08-07, Last modification date: 2024-08-21) |
| Primary citation | Hansen, K.H.,Byeon, C.H.,Liu, Q.,Drace, T.,Boesen, T.,Conway, J.F.,Andreasen, M.,Akbey, U. Structure of biofilm-forming functional amyloid PSM alpha 1 from Staphylococcus aureus. Proc.Natl.Acad.Sci.USA, 121:e2406775121-e2406775121, 2024 Cited by PubMed Abstract: Biofilm-protected pathogenic causes chronic infections that are difficult to treat. An essential building block of these biofilms are functional amyloid fibrils that assemble from phenol-soluble modulins (PSMs). PSMα1 cross-seeds other PSMs into cross-β amyloid folds and is therefore a key element in initiating biofilm formation. However, the paucity of high-resolution structures hinders efforts to prevent amyloid assembly and biofilm formation. Here, we present a 3.5 Å resolution density map of the major PSMα1 fibril form revealing a left-handed cross-β fibril composed of two C-symmetric U-shaped protofilaments whose subunits are unusually tilted out-of-plane. Monomeric α-helical PSMα1 is extremely cytotoxic to cells, despite the moderate toxicity of the cross-β fibril. We suggest mechanistic insights into the PSM functional amyloid formation and conformation transformation on the path from monomer-to-fibril formation. Details of PSMα1 assembly and fibril polymorphism suggest how utilizes functional amyloids to form biofilms and establish a framework for developing therapeutics against infection and antimicrobial resistance. PubMed: 39116134DOI: 10.1073/pnas.2406775121 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
Download full validation report
