9ATW
Structure of biofilm-forming functional amyloid PSMa1 from Staphylococcus aureus
これはPDB形式変換不可エントリーです。
9ATW の概要
| エントリーDOI | 10.2210/pdb9atw/pdb |
| EMDBエントリー | 43835 |
| 分子名称 | Phenol-soluble modulin alpha 1 peptide (1 entity in total) |
| 機能のキーワード | functional amyloid fibril, biofilm, bacterial biofilm, phenol soluble modulin alpha1, psma1, structural protein |
| 由来する生物種 | Staphylococcus aureus |
| タンパク質・核酸の鎖数 | 64 |
| 化学式量合計 | 144820.29 |
| 構造登録者 | Hansen, K.H.,Byeon, C.H.,Liu, Q.,Drace, T.,Boesen, T.,Conway, J.F.,Andreasen, M.,Akbey, U. (登録日: 2024-02-27, 公開日: 2024-08-07, 最終更新日: 2024-08-21) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.5 Å) |
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