9M6Y

Crystal structure of C1 domain from surface protein SlpM of Lactobacillus brevis

Summary for 9M6Y

• Entry DOI: 10.2210/pdb9m6y/pdb
• Descriptor: Surface layer protein SlpM (2 entities in total)
• Functional Keywords: self-assembly, surface protein, s-layer protein, dimerization, structural protein
• Biological source: Levilactobacillus brevis
• Total number of polymer chains: 2
• Total formula weight: 19268.80

Authors

Xue, Y.,Kang, X. (deposition date: 2025-03-08, release date: 2025-06-11)

Primary citation

Xue, Y.,Kang, X.
Crystal structure of the C1 domain of the surface-layer protein SlpM from Lactobacillus brevis: a module involved in protein self-assembly.
Acta Crystallogr.,Sect.F, 81:255-262, 2025

PubMed 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.

PubMed: 40371669
DOI: 10.1107/S2053230X25004194

Experimental method

X-RAY DIFFRACTION (1.7 Å)