6IWY

Crystal structure of the flagellar cap protein FliD from Helicobacter pylori

Summary for 6IWY

• Entry DOI: 10.2210/pdb6iwy/pdb
• Descriptor: Flagellar hook-associated protein 2 (2 entities in total)
• Functional Keywords: bacterial flagellar cap protein, structural protein
• Biological source: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
• Total number of polymer chains: 1
• Total formula weight: 43883.90

Authors

Cho, S.Y.,Song, W.S.,Yoon, S.I. (deposition date: 2018-12-08, release date: 2019-05-22, Last modification date: 2024-03-27)

Primary citation

Cho, S.Y.,Song, W.S.,Oh, H.B.,Kim, H.U.,Jung, H.S.,Yoon, S.I.
Structural analysis of the flagellar capping protein FliD from Helicobacter pylori.
Biochem.Biophys.Res.Commun., 514:98-104, 2019

PubMed Abstract: Helicobacter pylori is a pathogenic flagellated bacterium that infects the gastroduodenal mucosa and causes peptic ulcers in humans. FliD caps the distal end of the flagellar filament and is essential in filament growth. Moreover, FliD has been studied to diagnose and prevent H. pylori infection. Here, we report structure-based molecular studies of H. pylori FliD (hpFliD). A crystal structure of hpFliD at 2.6 Å resolution presents a four-domain (D2-D5) structure, where the D3 domain forms a central platform surrounded by the other three domains (D2, D4, and D5). hpFliD domains D2 and D3 structurally resemble those of FliD orthologs, whereas the D4 and D5 domains are exclusive to hpFliD. Moreover, our ELISA analysis using anti-H. pylori antibodies demonstrated that the hpFliD-specific D4 and D5 domains are highly antigenic compared to the D2 and D3 domains. Collectively, our structural and serological analyses underscore the structural role of hpFliD domains and provide a molecular basis for vaccine and diagnosis development.

PubMed: 31023530
DOI: 10.1016/j.bbrc.2019.04.065

Experimental method

X-RAY DIFFRACTION (2.6 Å)