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9GK2

Surface-layer (S-layer) PS2 protein from Corynebacterium glutamicum

Summary for 9GK2
Entry DOI10.2210/pdb9gk2/pdb
EMDB information51414
DescriptorPS2 (1 entity in total)
Functional Keywordss-layer, corynebacterium, surface, structural protein
Biological sourceCorynebacterium glutamicum
Total number of polymer chains18
Total formula weight858003.46
Authors
Sogues, A.,Remaut, H.,Sleutel, M. (deposition date: 2024-08-23, release date: 2024-10-02, Last modification date: 2026-03-04)
Primary citationSogues, A.,Sleutel, M.,Petit, J.,Megrian, D.,Bayan, N.,Wehenkel, A.M.,Remaut, H.
Cryo-EM structure and polar assembly of the PS2 S-layer of Corynebacterium glutamicum.
Proc.Natl.Acad.Sci.USA, 122:e2426928122-e2426928122, 2025
Cited by
PubMed Abstract: The polar-growing have a complex cell envelope architecture characterized by the presence of a specialized outer membrane composed of mycolic acids. In some , 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 ex vivo PS2 S-layers from the industrially important and determined its atomic structure by 3D cryo-EM 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 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.
PubMed: 40729392
DOI: 10.1073/pnas.2426928122
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.5 Å)
Structure validation

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