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6gow

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Crystal structure of the flagellin-FliS complex from Bacillus subtilis crystallized in spacegroup P22121

Structural highlights

6gow is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	5maw
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[A0A162QQD4_BACIU] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.[RuleBase:RU362073]

Publication Abstract from PubMed

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.

FliS/flagellin/FliW heterotrimer couples type III secretion and flagellin homeostasis.,Altegoer F, Mukherjee S, Steinchen W, Bedrunka P, Linne U, Kearns DB, Bange G Sci Rep. 2018 Aug 1;8(1):11552. doi: 10.1038/s41598-018-29884-8. PMID:30068950^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Altegoer F, Mukherjee S, Steinchen W, Bedrunka P, Linne U, Kearns DB, Bange G. FliS/flagellin/FliW heterotrimer couples type III secretion and flagellin homeostasis. Sci Rep. 2018 Aug 1;8(1):11552. doi: 10.1038/s41598-018-29884-8. PMID:30068950 doi:http://dx.doi.org/10.1038/s41598-018-29884-8