Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8KCL

Crystal Structure of M- and C-Domains of the shaft pilin LrpA from Ligilactobacillus ruminis - Triclinic form

Summary for 8KCL
Entry DOI10.2210/pdb8kcl/pdb
Related8KB2
DescriptorLPXTG-motif cell wall anchor domain protein (2 entities in total)
Functional Keywordsbackbone pilin, isopeptide bond, pili, gut bacteria, probiotic, cell adhesion
Biological sourceLigilactobacillus ruminis ATCC 25644
Total number of polymer chains1
Total formula weight28139.40
Authors
Prajapati, A.,Palva, A.,von Ossowski, I.,Krishnan, V. (deposition date: 2023-08-08, release date: 2024-07-10, Last modification date: 2024-07-17)
Primary citationPrajapati, 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: 38935340
DOI: 10.1107/S2059798324005114
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.47 Å)
Structure validation

227344

건을2024-11-13부터공개중

PDB statisticsPDBj update infoContact PDBjnumon