Bacterial flagellins: does only size matter?
Sergei Yu. ShchyogoleviD, Gennady Leonidovich BuryginiD, L. Yu. MatoraiD
Abstract
The protein sequences of a number of Azospirillaceae strains were investigated that contain the pf00669 domain and belong to a variety of bacterial flagellum systems with unusually large flagellin sizes. A set of tools for the homologous and template-based modeling of protein structures was used to reveal the probability of alternative folding, i.e., generation of two protein models with significantly different 3D structures and functions (flagellin or S-layer protein) for a single amino acid sequence.
02 /Specification & Classification
Click any tag to browse matching papers- Citations
- 0
- Organism
- Assay
- Research Focus
- Approach
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Structural modeling of the flagellum MS ring protein FliF reveals similarities to the type III secretion system and sporulation complex
Julien R. C. Bergeron·bioRxiv·Nov 4, 2015
- Giant flagellins form thick flagellar filaments in two species of marine γ-proteobacteria
N. M. Thomson, J. L. Ferreira, … M. J. Pallen·bioRxiv·Sep 20, 2018
- Structural diversity and clustering of bacterial flagellar outer domains
Jessie Lynda Fields, Hua Zhang, … Fengbin Wang·Nature CommunicationsPeer-reviewed·Nov 3, 2024
- Bacterial motility depends on a critical flagellum length and energy-optimised assembly
Manuel Halte, Philipp F. Popp, … Thibaud T. Renault·Proceedings of the National Academy of SciencesPeer-reviewed·Mar 11, 2025
- Oligomerization of the FliF domains suggests a coordinated assembly of the bacterial flagellum MS ring
G. Mariano, R. Faba-Rodriguez, … J. Bergeron·bioRxiv·Sep 23, 2021
- Structural diversity of oligomeric β-propellers with different numbers of identical blades
E. Afanasieva, I. Chaudhuri, … A. N. Lupas·bioRxiv·Aug 2, 2019