Abstract: Amyloids are structurally ordered protein aggregates involved in aggregation diseases as well as in physiological activities in humans and microbes. Structures of full-length amyloid proteins are rare and limited in resolution. Bacterial functional amyloids, in particular, have proceeded in a vacuum of structural knowledge. Our structural work on microbial amyloid peptides and spine segments show that the amyloid fold is far more diverse and rich in conformations than currently acknowledged, and suggest that we are only at the dawn of understanding the mystery of the amyloid and its structure-function relationships.