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  Interdigitated immunoglobulin arrays form the hyperstable surface layer of the extremophilic bacterium Deinococcus radiodurans

von Kügelgen, A., van Dorst, S., Yamashita, K., Sexton, D., Tocheva, E., Murshudov, G., et al. (2023). Interdigitated immunoglobulin arrays form the hyperstable surface layer of the extremophilic bacterium Deinococcus radiodurans. Proceedings of the National Academy of Sciences of the United States of America, 120(16): e2215808120. doi:10.1073/pnas.2215808120.

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von Kügelgen, A, Author
van Dorst, S, Author
Yamashita, K, Author
Sexton, DL, Author
Tocheva, EI, Author
Murshudov, G, Author
Alva, V1, 2, Author                 
Bharat, TAM, Author           
Affiliations:
1Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society, ou_3371683              
2Protein Bioinformatics Group, Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society, ou_3477399              

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 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 cryotomography and subtomogram averaging from focused ion beam-milled D. radiodurans 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 D. radiodurans 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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 Dates: 2023-04
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1073/pnas.2215808120
PMID: 37043530
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : PNAS
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: 8 Volume / Issue: 120 (16) Sequence Number: e2215808120 Start / End Page: - Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230