7QEC

Crystal structure of SlpA - domain II, domain that is involved in the self-assembly of the S-layer from Lactobacillus amylovorus

Summary for 7QEC

• Entry DOI: 10.2210/pdb7qec/pdb
• Descriptor: S-layer (2 entities in total)
• Functional Keywords: s-layer, self-assembly, lactobacillus amylovorus, structural protein
• Biological source: Lactobacillus amylovorus (strain GRL 1112)
• Total number of polymer chains: 1
• Total formula weight: 11641.81

Authors

Eder, M.,Dordic, A.,Millan, C.,Sagmeister, T.,Uson, I.,Pavkov-Keller, T. (deposition date: 2021-12-02, release date: 2022-12-14, Last modification date: 2024-06-19)

Primary citation

Sagmeister, T.,Gubensak, N.,Buhlheller, C.,Grininger, C.,Eder, M.,Ðordic, A.,Millan, C.,Medina, A.,Murcia, P.A.S.,Berni, F.,Hynonen, U.,Vejzovic, D.,Damisch, E.,Kulminskaya, N.,Petrowitsch, L.,Oberer, M.,Palva, A.,Malanovic, N.,Codee, J.,Keller, W.,Uson, I.,Pavkov-Keller, T.
The molecular architecture of Lactobacillus S-layer: Assembly and attachment to teichoic acids.
Proc.Natl.Acad.Sci.USA, 121:e2401686121-e2401686121, 2024

PubMed Abstract: S-layers are crystalline arrays found on bacterial and archaeal cells. is a diverse family of bacteria known especially for potential gut health benefits. This study focuses on the S-layer proteins from and common in the mammalian gut. Atomic resolution structures of S-layer proteins SlpA and SlpX exhibit domain swapping, and the obtained assembly model of the main S-layer protein SlpA aligns well with prior electron microscopy and mutagenesis data. The S-layer's pore size suggests a protective role, with charged areas aiding adhesion. A highly similar domain organization and interaction network are observed across the genus. Interaction studies revealed conserved binding areas specific for attachment to teichoic acids. The structure of the SlpA S-layer and the suggested incorporation of SlpX as well as its interaction with teichoic acids lay the foundation for deciphering its role in immune responses and for developing effective treatments for a variety of infectious and bacteria-mediated inflammation processes, opening opportunities for targeted engineering of the S-layer or lactobacilli bacteria in general.

PubMed: 38838019
DOI: 10.1073/pnas.2401686121

Experimental method

X-RAY DIFFRACTION (1.95 Å)