ArticleThe Journal of biological chemistry2022
The cryo-EM structure of the S-layer deinoxanthin-binding complex of Deinococcus radiodurans informs properties of its environmental interactions.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed.
- S-layer architecture and glycosylation and their role in shaping virus-host specificity in prokaryotes.Frontiers in microbiology · 2026Review
- A new age in structural S-layer biology: Experimental and in silico milestones.The Journal of biological chemistry · 2025Review
- Combining live fluorescence imaging with in situ cryoelectron tomography sheds light on the septation process inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural characterization and functional insights into the type II secretion system of the poly-extremophile Deinococcus radiodurans.The Journal of biological chemistry · 2024Article
- Insights into the synthesis, engineering, and functions of microbial pigments inFrontiers in microbiology · 2024Review
- Dual function of OmpM as outer membrane tether and nutrient uptake channel in diderm Firmicutes.Nature communications · 2023Article
- Extremophilic Solutions: The Role of Deinoxanthin in Counteracting UV-Induced Skin Harm.Current issues in molecular biology · 2023Article
- Interdigitated immunoglobulin arrays form the hyperstable surface layer of the extremophilic bacteriumProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Protein dynamics: The future is bright and complicated!Structural dynamics (Melville, N.Y.) · 2023Article
- Isolation and characterization of a main porin from the outer membrane of Salinibacter ruber.Journal of bioenergetics and biomembranes · 2022Article
- The structured organization ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- TMbed: transmembrane proteins predicted through language model embeddings.BMC bioinformatics · 2022Article
- Isolation and Characterization of Cell Envelope Fragments Comprising Archaeal S-Layer Proteins.Nanomaterials (Basel, Switzerland) · 2022Article
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Abstract
The radiation-resistant bacterium Deinococcus radiodurans is known as the world's toughest bacterium. The S-layer of D. radiodurans, consisting of several proteins on the surface of the cellular envelope and intimately associated with the outer membrane, has therefore been useful as a model for structural and functional studies. Its main proteinaceous unit, the S-layer deinoxanthin-binding complex (SDBC), is a hetero-oligomeric assembly known to contribute to the resistance against environmental stress and have porin functional features; however, its precise structure is unknown. Here, we resolved the structure of the SDBC at ∼2.5 Å resolution by cryo-EM and assigned the sequence of its main subunit, the protein DR_2577. This structure is characterized by a pore region, a massive β-barrel organization, a stalk region consisting of a trimeric coiled coil, and a collar region at the base of the stalk. We show that each monomer binds three Cu ions and one Fe ion and retains one deinoxanthin molecule and two phosphoglycolipids, all exclusive to D. radiodurans. Finally, electrophysiological characterization of the SDBC shows that it exhibits transport properties with several amino acids. Taken together, these results highlight the SDBC as a robust structure displaying both protection and sieving functions that facilitates exchanges with the environment.
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