Structural insights into the main S-layer unit of Deinococcus radiodurans reveal a massive protein complex with porin-like features.

ABSTRACT: In the extremophile bacterium Deinococcus radiodurans, the outermost surface layer is tightly connected with the rest of the cell wall. This integrated organization provides a compact structure that shields the bacterium against environmental stresses. The fundamental unit of this surface layer (S-layer) is the S-layer deinoxanthin-binding complex (SDBC), which binds the carotenoid deinoxanthin and provides both, thermostability and UV radiation resistance. However, the structural organization of the SDBC awaits elucidation. Here, we report the isolation of the SDBC with a gentle procedure consisting of lysozyme treatment and solubilization with the nonionic detergent n-dodecyl-β-d-maltoside, which preserved both hydrophilic and hydrophobic components of the SDBC and allows t

SUBMITTER: Farci D 

PROVIDER: S-EPMC7105295 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature