9GK2
Surface-layer (S-layer) PS2 protein from Corynebacterium glutamicum
Summary for 9GK2
| Entry DOI | 10.2210/pdb9gk2/pdb |
| EMDB information | 51414 |
| Descriptor | PS2 (1 entity in total) |
| Functional Keywords | s-layer, corynebacterium, surface, structural protein |
| Biological source | Corynebacterium glutamicum |
| Total number of polymer chains | 18 |
| Total formula weight | 858003.46 |
| Authors | |
| Primary citation | Sogues, 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. Biorxiv, 2024 Cited by PubMed Abstract: 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. PubMed: 39282302DOI: 10.1101/2024.09.05.611363 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.5 Å) |
Structure validation
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