8KCL
Crystal Structure of M- and C-Domains of the shaft pilin LrpA from Ligilactobacillus ruminis - Triclinic form
8KCL の概要
エントリーDOI | 10.2210/pdb8kcl/pdb |
関連するPDBエントリー | 8KB2 |
分子名称 | LPXTG-motif cell wall anchor domain protein (2 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 | 28139.40 |
構造登録者 | Prajapati, A.,Palva, A.,von Ossowski, I.,Krishnan, V. (登録日: 2023-08-08, 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 Cited by 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: 38935340DOI: 10.1107/S2059798324005114 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.47 Å) |
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