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-Structure paper
| タイトル | Allosteric amyloid catalysis by coiled coil fibrils. |
|---|---|
| ジャーナル・号・ページ | Nat Commun, Vol. 16, Issue 1, Page 5071, Year 2025 |
| 掲載日 | 2025年5月31日 |
著者 | Sisira Mambram Kunnath / Elad Arad / Ran Zalk / Itamar Kass / Anat Shahar / Albert Batushansky / Hanna Rapaport / Raz Jelinek / ![]() |
| PubMed 要旨 | Amyloid-mediated catalysis of key biological reactions has recently attracted significant interest as this phenomenon may portend new functions for physiological and synthetic amyloid proteins. Here, ...Amyloid-mediated catalysis of key biological reactions has recently attracted significant interest as this phenomenon may portend new functions for physiological and synthetic amyloid proteins. Here, we report an allosteric mechanism of catalytic amyloids, mediated via an unconventional coiled-coil fibril organization, facilitating hydrolysis of β-lactam antibiotics. Specifically, the hydrolysis reaction was catalyzed by a fibrillar peptide comprising alternating lysine/phenylalanine β-sheet-forming sequence. Analysis of peptide variants, simulations, and cryogenic electron microscopy reveal that the β-lactam molecules attach electrostatically to the lysine sidechains on the fibrils' surfaces, generating a double-coiled fibril structure in which the anchored β-lactam molecules are nestled within twisted fibril strands. This organization facilitates the allosteric catalytic process in which hydrolytic β-lactam ring opening is induced via nucleophilic attacks by the lysine sidechains degradation. The allosteric catalytic activity of the phenylalanine/lysine amyloid fibrils highlights the functional versatility of amyloid fibrils and their potential applications in human health and environmental biotechnology. |
リンク | Nat Commun / PubMed:40450012 / PubMed Central |
| 手法 | EM (らせん対称) |
| 解像度 | 5.0 Å |
| 構造データ | EMDB-53305, PDB-9r7e: |
| 化合物 | ![]() ChemComp-NEF: |
| 由来 |
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キーワード | PROTEIN FIBRIL / Allosteric amyloid coiled-coil fibrils |
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anaeramoeba ignava (真核生物)
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