Crystal Structure of the C-Terminal Domain of a Flagellar Hook-Capping Protein from Xanthomonas campestris

Crystal structure of a novel dimer form of FlgD from P. aeruginosa PAO1

“…The N‐terminal region of FlgD, which is much more flexible and more susceptible to proteolytic cleavage than the C‐terminal region, might serve as a secretory signal to help the flagellar protein arrive at target location. This has been shown to be the case for other flagellar proteins 9, 21…”

“…Additionally, SDS‐PAGE gel experiments confirmed that the crystal was a fragment protein with molecular weight 15 kDa and about 10 kDa segments had been degraded (unpublished data). Interestingly, the N‐terminus of FlgD from Xanthomonas campestris (XcFlgD), corresponding to residues 84–220, was also disordered in that crystal structure (Kuo et al 9…”

“…To assess the degree of structural similarity, we compared the structure of PaFlgD with the structure of its homolog from Xanthomonas campestris 9. PaFlgD superimposes onto the XcFlgD structure with a calculated r.m.s.d.…”

“…This structure comprises a novel hybrid fold consisting of a tudor‐like domain and a fibronectin type III domain. XcFlgD forms three types of dimers in the crystal 9. Efforts in our laboratory to study the structure of FlgD from P. aeruginosa PAO1 (PaFlgD) have yielded an alterative arrangement of the FlgD homodimer that differs substantially from that previous described.…”

Structural Characterization at the Atomic Level of a Molecular Nano-Machine: The State of the Art of <i>Helicobacter Pylori</i> Flagellum Organization

“…pylori FlgD is composed of 301 amino acid residues. By now, two crystal structures of FlgD have been solved, from P. aeruginosa (PDB ID 3OSV; (Zhou et al, 2011)) and X. campestris (PDB ID 3C12; (Kuo et al, 2008)). Both structures do not include the N-terminal domain, largely flexible.…”