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TitleStructural analysis of the architecture and in situ localization of the main S-layer complex in Deinococcus radiodurans.
Journal, issue, pagesStructure, Vol. 29, Issue 11, Page 1279-11285.e3, Year 2021
Publish dateNov 4, 2021
AuthorsDomenica Farci / Sami Kereïche / Sushil Pangeni / Patrycja Haniewicz / Igor V Bodrenko / Matteo Ceccarelli / Mathias Winterhalter / Dario Piano /
PubMed AbstractBacterial surface layers are paracrystalline assemblies of proteins that provide the first line of defense against environmental shocks. Here, we report the 3D structure, in situ localization, and ...Bacterial surface layers are paracrystalline assemblies of proteins that provide the first line of defense against environmental shocks. Here, we report the 3D structure, in situ localization, and orientation of the S-layer deinoxanthin-binding complex (SDBC), a hetero-oligomeric assembly of proteins that in Deinococcus radiodurans represents the main S-layer unit. The SDBC is resolved at 11-Å resolution by single-particle analysis, while its in situ localization is determined by cryo-electron crystallography on intact cell-wall fragments leading to a projection map at 4.5-Å resolution. The SDBC exhibits a triangular base with three comma-shaped pores, and a stalk departing orthogonally from the center of the base and oriented toward the intracellular space. Combining state-of-the-art techniques, results show the organization of this S-layer and its connection within the underlying membranes, demonstrating the potential for applications from nanotechnologies to medicine.
External linksStructure / PubMed:34265277
MethodsEM (single particle)
Resolution11.0 Å
Structure data

EMDB-12169:
S-layer Deinoxanthin Binding Complex (SDBC)
Method: EM (single particle) / Resolution: 11.0 Å

Source
  • Deinococcus radiodurans R1 (radioresistant)

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