Interdigitated immunoglobulin arrays form the hyperstable surface layer of the extremophilic bacterium <i>Deinococcus radiodurans</i>.

ABSTRACT: Deinococcus radiodurans is an atypical diderm bacterium with a remarkable ability to tolerate various environmental stresses, due in part to its complex cell envelope encapsulated within a hyperstable surface layer (S-layer). Despite decades of research on this cell envelope, atomic structural details of the S-layer have remained obscure. In this study, we report the electron cryomicroscopy structure of the D. radiodurans S-layer, showing how it is formed by the Hexagonally Packed Intermediate-layer (HPI) protein arranged in a planar hexagonal lattice. The HPI protein forms an array of immunoglobulin-like folds within the S-layer, with each monomer extending into the adjacent hexamer, resulting in a highly interconnected, stable, sheet-like arrangement. Using electron cryotom

SUBMITTER: von Kugelgen A 

PROVIDER: S-EPMC10120038 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature