2N59
Solution Structure of R. palustris CsgH
2N59 の概要
| エントリーDOI | 10.2210/pdb2n59/pdb |
| NMR情報 | BMRB: 25700 |
| 分子名称 | Putative uncharacterized protein CsgH (1 entity in total) |
| 機能のキーワード | unknown function |
| 由来する生物種 | Rhodopseudomonas palustris DX-1 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 11183.52 |
| 構造登録者 | Hawthorne, W.J.,Taylor, J.D.,Escalera-Maurer, A.,Lambert, S.,Koch, M.,Scull, N.,Sefer, L.,Xu, Y.,Matthews, S.J. (登録日: 2015-07-13, 公開日: 2016-05-11, 最終更新日: 2024-11-20) |
| 主引用文献 | Taylor, J.D.,Hawthorne, W.J.,Lo, J.,Dear, A.,Jain, N.,Meisl, G.,Andreasen, M.,Fletcher, C.,Koch, M.,Darvill, N.,Scull, N.,Escalera-Maurer, A.,Sefer, L.,Wenman, R.,Lambert, S.,Jean, J.,Xu, Y.,Turner, B.,Kazarian, S.G.,Chapman, M.R.,Bubeck, D.,de Simone, A.,Knowles, T.P.,Matthews, S.J. Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones. Sci Rep, 6:24656-24656, 2016 Cited by PubMed Abstract: Polypeptide aggregation into amyloid is linked with several debilitating human diseases. Despite the inherent risk of aggregation-induced cytotoxicity, bacteria control the export of amyloid-prone subunits and assemble adhesive amyloid fibres during biofilm formation. An Escherichia protein, CsgC potently inhibits amyloid formation of curli amyloid proteins. Here we unlock its mechanism of action, and show that CsgC strongly inhibits primary nucleation via electrostatically-guided molecular encounters, which expands the conformational distribution of disordered curli subunits. This delays the formation of higher order intermediates and maintains amyloidogenic subunits in a secretion-competent form. New structural insight also reveal that CsgC is part of diverse family of bacterial amyloid inhibitors. Curli assembly is therefore not only arrested in the periplasm, but the preservation of conformational flexibility also enables efficient secretion to the cell surface. Understanding how bacteria safely handle amyloidogenic polypeptides contribute towards efforts to control aggregation in disease-causing amyloids and amyloid-based biotechnological applications. PubMed: 27098162DOI: 10.1038/srep24656 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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