5FHY
Crystal structure of FliD (HAP2) from Pseudomonas aeruginosa PAO1
Summary for 5FHY
| Entry DOI | 10.2210/pdb5fhy/pdb |
| Descriptor | B-type flagellar hook-associated protein 2, SODIUM ION (3 entities in total) |
| Functional Keywords | bacterial flagella, cap protein, structural protein |
| Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) |
| Cellular location | Secreted: Q9K3C5 |
| Total number of polymer chains | 2 |
| Total formula weight | 71820.44 |
| Authors | Postel, S.,Bonsor, D.,Diederichs, K.,Sundberg, E.J. (deposition date: 2015-12-22, release date: 2016-10-05, Last modification date: 2024-04-03) |
| Primary citation | Postel, S.,Deredge, D.,Bonsor, D.A.,Yu, X.,Diederichs, K.,Helmsing, S.,Vromen, A.,Friedler, A.,Hust, M.,Egelman, E.H.,Beckett, D.,Wintrode, P.L.,Sundberg, E.J. Bacterial flagellar capping proteins adopt diverse oligomeric states. Elife, 5:-, 2016 Cited by PubMed Abstract: Flagella are crucial for bacterial motility and pathogenesis. The flagellar capping protein (FliD) regulates filament assembly by chaperoning and sorting flagellin (FliC) proteins after they traverse the hollow filament and exit the growing flagellum tip. In the absence of FliD, flagella are not formed, resulting in impaired motility and infectivity. Here, we report the 2.2 Å resolution X-ray crystal structure of FliD from , the first high-resolution structure of any FliD protein from any bacterium. Using this evidence in combination with a multitude of biophysical and functional analyses, we find that FliD exhibits unexpected structural similarity to other flagellar proteins at the domain level, adopts a unique hexameric oligomeric state, and depends on flexible determinants for oligomerization. Considering that the flagellin filaments on which FliD oligomers are affixed vary in protofilament number between bacteria, our results suggest that FliD oligomer stoichiometries vary across bacteria to complement their filament assemblies. PubMed: 27664419DOI: 10.7554/eLife.18857 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.201 Å) |
Structure validation
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