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8C50

Pontibacter korlensis curli subunit CsgA

Summary for 8C50
Entry DOI10.2210/pdb8c50/pdb
EMDB information16431
DescriptorCurlin associated repeat-containing protein (1 entity in total)
Functional Keywordsbacterial functional amyloid, protein fibril
Biological sourcePontibacter korlensis
Total number of polymer chains3
Total formula weight114101.36
Authors
Remaut, H.,Sleutel, M.,Pradhan, B. (deposition date: 2023-01-05, release date: 2023-06-28, Last modification date: 2024-07-24)
Primary citationSleutel, M.,Pradhan, B.,Volkov, A.N.,Remaut, H.
Structural analysis and architectural principles of the bacterial amyloid curli.
Nat Commun, 14:2822-2822, 2023
Cited by
PubMed Abstract: Two decades have passed since the initial proposition that amyloids are not only (toxic) byproducts of an unintended aggregation cascade, but that they can also be produced by an organism to serve a defined biological function. That revolutionary idea was borne out of the realization that a large fraction of the extracellular matrix that holds Gram-negative cells into a persistent biofilm is composed of protein fibers (curli; tafi) with cross-β architecture, nucleation-dependent polymerization kinetics and classic amyloid tinctorial properties. The list of proteins shown to form so-called functional amyloid fibers in vivo has greatly expanded over the years, but detailed structural insights have not followed at a similar pace in part due to the associated experimental barriers. Here we combine extensive AlphaFold2 modelling and cryo-electron transmission microscopy to propose an atomic model of curli protofibrils, and their higher modes of organization. We uncover an unexpected structural diversity of curli building blocks and fibril architectures. Our results allow for a rationalization of the extreme physico-chemical robustness of curli, as well as earlier observations of inter-species curli promiscuity, and should facilitate further engineering efforts to expand the repertoire of curli-based functional materials.
PubMed: 37198180
DOI: 10.1038/s41467-023-38204-2
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7.6 Å)
Structure validation

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