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-Structure paper
タイトル | Interdigitated immunoglobulin arrays form the hyperstable surface layer of the extremophilic bacterium . |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 120, Issue 16, Page e2215808120, Year 2023 |
掲載日 | 2023年4月18日 |
![]() | Andriko von Kügelgen / Sofie van Dorst / Keitaro Yamashita / Danielle L Sexton / Elitza I Tocheva / Garib Murshudov / Vikram Alva / Tanmay A M Bharat / ![]() ![]() ![]() |
PubMed 要旨 | 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- ... 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 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 cryotomography and subtomogram averaging from focused ion beam-milled cells, we have obtained a structure of the cellular S-layer, showing how this HPI S-layer coats native membranes on the surface of cells. Our S-layer structure from the diderm bacterium shows similarities to immunoglobulin-like domain-containing S-layers from monoderm bacteria and archaea, highlighting common features in cell surface organization across different domains of life, with connotations on the evolution of immunoglobulin-based molecular recognition systems in eukaryotes. |
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手法 | EM (単粒子) |
解像度 | 2.52 Å |
構造データ | EMDB-16694, PDB-8cka: |
由来 |
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![]() | STRUCTURAL PROTEIN / HPI S-layer |