5MAW

Crystal structure of the flagellin-FliS complex from Bacillus subtilis

Summary for 5MAW

• Entry DOI: 10.2210/pdb5maw/pdb
• Descriptor: Flagellin, Flagellar protein 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: 48691.25

Authors

Altegoer, F.,Bange, G. (deposition date: 2016-11-07, release date: 2017-12-20, 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

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: 30068950
DOI: 10.1038/s41598-018-29884-8

Experimental method

X-RAY DIFFRACTION (1.5 Å)