9M6Y

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

9M6Y の概要

• エントリーDOI: 10.2210/pdb9m6y/pdb
• 分子名称: Surface layer protein SlpM (2 entities in total)
• 機能のキーワード: self-assembly, surface protein, s-layer protein, dimerization, structural protein
• 由来する生物種: Levilactobacillus brevis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19268.80

構造登録者

Xue, Y.,Kang, X. (登録日: 2025-03-08, 公開日: 2025-06-11)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.7 Å)