Tetrameric structure of the flagellar cap protein FliD from Serratia marcescens

Biochemical and Biophysical Research Communications
So Yeon ChoSung-Il Yoon

Abstract

Bacterial motility is provided by the flagellum. FliD is located at the distal end of the flagellum and plays a key role in the insertion of each flagellin protein at the growing tip of the flagellar filament. Because FliD functions as an oligomer, the determination of the oligomeric state of FliD is critical to understanding the molecular mechanism of FliD-mediated flagellar growth. FliD has been shown to adopt a pentameric or a hexameric structure depending on the bacterial species. Here, we report another distinct oligomeric form of FliD based on structural and biochemical studies. The crystal structures of the D2 and D3 domains of Serratia marcescens FliD (smFliD) were determined in two crystal forms and together revealed that smFliD assembles into a tetrameric architecture that resembles a four-pointed star plate. smFliD tetramerization was also confirmed in solution by cross-linking experiments. Although smFliD oligomerizes in a head-to-tail orientation using a common primary binding interface between the D2 and D3' domains (the prime denotes the second subunit in the oligomer) similarly to other FliD orthologs, the smFliD tetramer diverges to present a unique secondary D2-D2' binding interface. Our structure-based compar...Continue Reading

References

Dec 23, 2016·Cellular Microbiology·Claudia M FreitagJos P M van Putten

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Citations

Dec 14, 2017·Biophysics Reviews·Katsumi Imada
Sep 27, 2018·Scientific Reports·Ho Jeong HongSung-Il Yoon
Sep 23, 2019·Biochemical and Biophysical Research Communications·So Yeon ChoSung-Il Yoon
Jul 25, 2021·International Journal of Molecular Sciences·Marko NedeljkovićEric John Sundberg

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