The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.

ABSTRACT: Amyloids, once viewed solely as pathological hallmarks, are now recognized as widespread and versatile functional protein assemblies. Bacterial functional amyloids (FuBAs), particularly curli (CsgA) from Escherichia coli and FapC from Pseudomonas, have emerged as paradigms for understanding amyloid structure, assembly, and function. The recent cryo-EM-based structure of FapC, together with others' combined cryo-EM and integrative computational studies on CsgA, reveal a β-solenoid fold stabilized by imperfect repeats, producing fibrils of exceptional stability and low polymorphism, whose biogenesis is tightly controlled through dedicated accessory factors, ensuring precise secretion and nucleation. FuBAs not only scaffold biofilms but also display intrinsic catalytic activity, expanding the

SUBMITTER: Pena-Diaz S 

PROVIDER: S-EPMC12822426 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature