6GOW
Crystal structure of the flagellin-FliS complex from Bacillus subtilis crystallized in spacegroup P22121
Summary for 6GOW
| Entry DOI | 10.2210/pdb6gow/pdb |
| Related | 5MAW |
| Descriptor | Flagellin, Flagellar secretion chaperone FliS (3 entities in total) |
| Functional Keywords | flagellum, type-3-secretion, chaperone |
| Biological source | Bacillus subtilis More |
| Total number of polymer chains | 2 |
| Total formula weight | 47805.32 |
| Authors | Altegoer, F.,Bange, G. (deposition date: 2018-06-04, release date: 2018-08-29, Last modification date: 2024-01-17) |
| Primary citation | Altegoer, F.,Mukherjee, S.,Steinchen, W.,Bedrunka, P.,Linne, U.,Kearns, D.B.,Bange, G. FliS/flagellin/FliW heterotrimer couples type III secretion and flagellin homeostasis. Sci Rep, 8:11552-11552, 2018 Cited by PubMed Abstract: Flagellin is amongst the most abundant proteins in flagellated bacterial species and constitutes the major building block of the flagellar filament. The proteins FliW and FliS serve in the post-transcriptional control of flagellin and guide the protein to the flagellar type III secretion system (fT3SS), respectively. Here, we present the high-resolution structure of FliS/flagellin heterodimer and show that FliS and FliW bind to opposing interfaces located at the N- and C-termini of flagellin. The FliS/flagellin/FliW heterotrimer is able to interact with FlhA-C suggesting that FliW and FliS are released during flagellin export. After release, FliW and FliS are recycled to execute a new round of post-transcriptional regulation and targeting. Taken together, our study provides a mechanism explaining how FliW and FliS synchronize the production of flagellin with the capacity of the fT3SS to secrete flagellin. PubMed: 30068950DOI: 10.1038/s41598-018-29884-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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