2N59

Solution Structure of R. palustris CsgH

Summary for 2N59

• Entry DOI: 10.2210/pdb2n59/pdb
• NMR Information: BMRB: 25700
• Descriptor: Putative uncharacterized protein CsgH (1 entity in total)
• Functional Keywords: unknown function
• Biological source: Rhodopseudomonas palustris DX-1
• Total number of polymer chains: 1
• Total formula weight: 11183.52

Authors

Hawthorne, W.J.,Taylor, J.D.,Escalera-Maurer, A.,Lambert, S.,Koch, M.,Scull, N.,Sefer, L.,Xu, Y.,Matthews, S.J. (deposition date: 2015-07-13, release date: 2016-05-11, Last modification date: 2024-11-20)

Primary citation

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

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: 27098162
DOI: 10.1038/srep24656

Experimental method

SOLUTION NMR