8KG4
Crystal Structure of M- and C-Domains of the shaft pilin LrpA from Ligilactobacillus ruminis - orthorhombic form
Summary for 8KG4
Entry DOI | 10.2210/pdb8kg4/pdb |
Related | 8KB2 8KCL |
Descriptor | LPXTG-motif cell wall anchor domain protein, IODIDE ION, SODIUM ION, ... (6 entities in total) |
Functional Keywords | backbone pilin, isopeptide bond, pili, gut bacteria, probiotic, cell adhesion |
Biological source | Ligilactobacillus ruminis ATCC 25644 |
Total number of polymer chains | 1 |
Total formula weight | 30336.20 |
Authors | Prajapati, A.,Palva, A.,von Ossowski, I.,Krishnan, V. (deposition date: 2023-08-17, release date: 2024-07-10, Last modification date: 2024-07-17) |
Primary citation | 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 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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