Crystal structure of a novel dimer form of FlgD from <i>P. aeruginosa</i> PAO1

Zhou, Hua; Luo, Miao; Cai, Xue-Fei; Niu, Siqiang; Zhang, Wenlu; Hu, Yuan; Yin, Yibing; Huang, Aiping; Wang, Dacheng; Wang, Deqiang

doi:10.1002/prot.23058

Cited by 9 publications

(7 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Other bacterial orthologues of the FlgD protein, whose crystal structures have been solved (XcFlgD, PaFlgD), [5,7] show the same tendency to lose the Nterminal part during crystallization. The HpFlgD sequence contains an extra 44 and 29 amino acids at the C-terminus in the G27 and 26695 strains, respectively in comparison to XcFlgD and PaFlgD.…”

Section: Crystal Structure Of the Monoclinic Form Of Hpflgd_26695 Andmentioning

confidence: 99%

“…[5,7,8] H. pylori survives in the stomach environment at pH 4−6.5. The FlgD protein is a hook-capping protein and, similarly to other H. pylori flagellar proteins, is predicted to have a pI value of around 5.…”

Section: Stability Of Hpflgd_26695 In Solutionmentioning

confidence: 99%

“…). [7] Amino acid residues used for the torsion angle calculation are highlighted in dark purple and dark blue in HpFlgD_26695_m and PaFlgD, respectively. (Figure 5b).…”

Section: Stability Of Hpflgd_26695 In Solutionmentioning

confidence: 99%

“…[5] Moreover, FlgD interacts with FliK and FlhB and regulates appropriate assembly of FlgE monomers in the hook structure. [6] Until now crystal structures of two other FlgD homologues, from Xanthomonas campestris (XcFlgD, PDB code: 3C12) [5] and Pseudomonas aeruginosa (PaFlgD, PDB code: 3OSV), [7] have been determined, as well as two crystal structures of H. pylori FlgD from two different strains and in two different space groups (HpFlgD_26695_t, tetragonal space group I422, and HpFlgD_G27_m, monoclinic space group P2, with PDB codes 4ZZF and 4ZZK, respectively). [8] In this paper we describe the crystal structure of truncated FlgD from the H. pylori strain 26695 in a new space group, and discuss stability of the full length protein.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Structure and Stability of FlgD from the Pathogenic 26695 Strain of Helicobacter pylori

et al. 2016

View full text Add to dashboard Cite

Flagellin component D (FlgD) is a hook capping protein involved in the proper structural assembly of bacterial flagella but is not present in the mature flagella. We report here the crystal structure of the truncated form of FlgD from the strain 26695 of Helicobacter pylori (HpFlgD_26695) in the P2 space group at 2.8 Å resolution, along with data on protein stability. The structure includes only the central globular part of the protein composed of conserved Fn-III and tudor domains, while the N-and C-terminal regions are absent. This structure, together with the tetragonal crystal structure of HpFlgD_26695 and the monoclinic crystal structure of HpFlgD_G27 reported previously, revealed a different mutual orientation of the two domains in the HpFlgD structures in respect to FlgD from Xanthomonas campestris and Pseudomonas aeruginosa. In addition, investigation of protein stability in solution showed higher protein stability then in other bacterial orthologues reported so far.

show abstract

Section: Crystal Structure Of the Monoclinic Form Of Hpflgd_26695 Andmentioning

confidence: 99%

Section: Stability Of Hpflgd_26695 In Solutionmentioning

confidence: 99%

“…). [7] Amino acid residues used for the torsion angle calculation are highlighted in dark purple and dark blue in HpFlgD_26695_m and PaFlgD, respectively. (Figure 5b).…”

Section: Stability Of Hpflgd_26695 In Solutionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Structure and Stability of FlgD from the Pathogenic 26695 Strain of Helicobacter pylori

et al. 2016

View full text Add to dashboard Cite

show abstract

“…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.…”

Section: The Hookmentioning

confidence: 99%

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

Pulić¹,

Loconte²,

Zanotti³

2014

American Journal of Biochemistry and Biotechnology

View full text Add to dashboard Cite

Motility is fundamental for success in colonization and survival of the human pathogen H. pylori, the bacterium that colonizes about half of the human population. Motility is achieved through flagella. In this review the present structural knowledge about the organization of H. pylori flagella is summarized, considering not only the structure of its proteins, but also what is known about flagella of other Gram-negative bacteria. Despite the limited amount of structural information about the H. pylori nano-machinery, sequence alignments and homology modeling allow to investigate the unique structural properties of several H. pylori flagellar proteins.

show abstract

An overview of the structure and function of the flagellar hook FlgE protein

You

Mao

et al. 2023

World J Microbiol Biotechnol

View full text Add to dashboard Cite

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

Cited by 9 publications

References 23 publications

Structure and Stability of FlgD from the Pathogenic 26695 Strain of Helicobacter pylori

Structure and Stability of FlgD from the Pathogenic 26695 Strain of Helicobacter pylori

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

An overview of the structure and function of the flagellar hook FlgE protein

Contact Info

Product

Resources

About