8CKA
Deinococcus radidurans HPI S-layer
Summary for 8CKA
| Entry DOI | 10.2210/pdb8cka/pdb |
| EMDB information | 16694 |
| Descriptor | Hexagonally packed intermediate-layer surface protein (1 entity in total) |
| Functional Keywords | hpi s-layer, structural protein |
| Biological source | Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) |
| Total number of polymer chains | 2 |
| Total formula weight | 198848.00 |
| Authors | von Kuegelgen, A.,Yamashita, K.,Murshudov, G.,Bharat, T. (deposition date: 2023-02-14, release date: 2023-04-19, Last modification date: 2024-10-23) |
| Primary citation | von Kugelgen, A.,van Dorst, S.,Yamashita, K.,Sexton, D.L.,Tocheva, E.I.,Murshudov, G.,Alva, V.,Bharat, T.A.M. Interdigitated immunoglobulin arrays form the hyperstable surface layer of the extremophilic bacterium Deinococcus radiodurans. Proc.Natl.Acad.Sci.USA, 120:e2215808120-e2215808120, 2023 Cited by PubMed Abstract: 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. PubMed: 37043530DOI: 10.1073/pnas.2215808120 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.52 Å) |
Structure validation
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