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TitleCryo-EM structure and polar assembly of the PS2 S-layer of .
Journal, issue, pagesbioRxiv, Year 2024
Publish dateSep 5, 2024
AuthorsAdrià Sogues / Mike Sleutel / Julienne Petit / Daniela Megrian / Nicolas Bayan / Anne Marie Wehenkel / Han Remaut /
PubMed AbstractThe polar-growing Corynebacteriales have a complex cell envelope architecture characterized by the presence of a specialized outer membrane composed of mycolic acids. In some Corynebacteriales, this ...The polar-growing Corynebacteriales have a complex cell envelope architecture characterized by the presence of a specialized outer membrane composed of mycolic acids. In some Corynebacteriales, this mycomembrane is further supported by a proteinaceous surface layer or 'S-layer', whose function, structure and mode of assembly remain largely enigmatic. Here, we isolated PS2 S-layers from the industrially important and determined its atomic structure by 3D cryoEM reconstruction. PS2 monomers consist of a six-helix bundle 'core', a three-helix bundle 'arm', and a C-terminal transmembrane (TM) helix. The PS2 core oligomerizes into hexameric units anchored in the mycomembrane by a channel-like coiled-coil of the TM helices. The PS2 arms mediate trimeric lattice contacts, crystallizing the hexameric units into an intricate semipermeable lattice. Using pulse-chase live cell imaging, we show that the PS2 lattice is incorporated at the poles, coincident with the actinobacterial elongasome. Finally, phylogenetic analysis shows a paraphyletic distribution and dispersed chromosomal location of PS2 in Corynebacteriales as a result of multiple recombination events and losses. These findings expand our understanding of S-layer biology and enable applications of membrane-supported self-assembling bioengineered materials.
External linksbioRxiv / PubMed:39282302 / PubMed Central
MethodsEM (single particle)
Resolution2.5 Å
Structure data

51414

9gk2

EMDB-51414, PDB-9gk2:
Surface-layer (S-layer) PS2 protein from Corynebacterium glutamicum
Method: EM (single particle) / Resolution: 2.5 Å

Source
  • corynebacterium glutamicum (bacteria)
KeywordsSTRUCTURAL PROTEIN / S-layer / Corynebacterium / Surface

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