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Most prokaryotic cells are encased in a surface layer (S-layer) consisting of a paracrystalline array of repeating lattice-forming proteins. S-layer proteins populate a vast and diverse sequence space, performing disparate functions in prokaryotic cells, including cellular defense, cell-shape maintenance, and regulation of import and export of materials. This article highlights recent advances in the understanding of S-layer structure and assembly, made possible by rapidly evolving structural and cell biology methods. We underscore shared assembly principles revealed by recent work and discuss a common molecular framework that may be used to understand the structural organization of S-layer proteins across bacteria and archaea.

Original publication




Journal article


Trends Microbiol

Publication Date





405 - 415


bacterial cell envelopes, bioinformatics, protein evolution, structural biology, surface layer, Archaea, Archaeal Proteins, Bacteria, Bacterial Proteins, Membrane Glycoproteins