ArticleActa crystallographica. Section F, Structural biology communications2025
Crystal structure of the C1 domain of the surface-layer protein SlpM from Lactobacillus brevis: a module involved in protein self-assembly.
Article in Acta crystallographica. Section F, Structural biology communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Surface-layer proteins (SLPs) play a crucial role in the self-assembly of bacterial surface layers, yet the structural details of their assembly domains remain largely unexplored. Here, we report the crystal structure of SlpM_C1, a structural module within the self-assembly domain of SlpM from Lactobacillus brevis. SlpM_C1 adopts a β-grasp fold, a conserved structural motif found in diverse protein families. Structural comparisons with ubiquitin and the SlpA_II domain from L. acidophilus reveal both shared and distinct features, highlighting elements of structural convergence despite sequence divergence. Furthermore, the dimerization patterns of SlpM_C1 and SlpA_II are compared and discussed. These findings provide new insights into the architecture and evolutionary adaptability of SLPs in Lactobacillus species.
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