8KB2

Crystal Structure of M- and C-Domains of the shaft pilin LrpA from Ligilactobacillus ruminis - iodide derivative

8KB2 の概要

• エントリーDOI: 10.2210/pdb8kb2/pdb
• 分子名称: LPXTG-motif cell wall anchor domain protein, IODIDE ION, SODIUM ION, ... (7 entities in total)
• 機能のキーワード: backbone pilin, isopeptide bond, pili, gut bacteria, probiotic, cell adhesion
• 由来する生物種: Ligilactobacillus ruminis ATCC 25644
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30717.56

構造登録者

Prajapati, A.,Palva, A.,von Ossowski, I.,Krishnan, V. (登録日: 2023-08-03, 公開日: 2024-07-10, 最終更新日: 2024-07-17)

主引用文献

Prajapati, A.,Palva, A.,von Ossowski, I.,Krishnan, V.
The crystal structure of the N-terminal domain of the backbone pilin LrpA reveals a new closure-and-twist motion for assembling dynamic pili in Ligilactobacillus ruminis.
Acta Crystallogr D Struct Biol, 80:474-492, 2024

PubMed Abstract: Sortase-dependent pili are long surface appendages that mediate attachment, colonization and biofilm formation in certain genera and species of Gram-positive bacteria. Ligilactobacillus ruminis is an autochthonous gut commensal that relies on sortase-dependent LrpCBA pili for host adherence and persistence. X-ray crystal structure snapshots of the backbone pilin LrpA were captured in two atypical bent conformations leading to a zigzag morphology in the LrpCBA pilus structure. Small-angle X-ray scattering and structural analysis revealed that LrpA also adopts the typical linear conformation, resulting in an elongated pilus morphology. Various conformational analyses and biophysical experiments helped to demonstrate that a hinge region located at the end of the flexible N-terminal domain of LrpA facilitates a new closure-and-twist motion for assembling dynamic pili during the assembly process and host attachment. Further, the incongruent combination of flexible domain-driven conformational dynamics and rigid isopeptide bond-driven stability observed in the LrpCBA pilus might also extend to the sortase-dependent pili of other bacteria colonizing a host.

PubMed: 38935340
DOI: 10.1107/S2059798324005114

実験手法

X-RAY DIFFRACTION (1.91 Å)