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PDBsum entry 5npy
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Motor protein
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PDB id
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5npy
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References listed in PDB file
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Key reference
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Title
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Structural characterization of flge2 protein from helicobacter pylori hook.
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Authors
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V.Loconte,
I.Kekez,
D.Matković-ČAlogović,
G.Zanotti.
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Ref.
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FEBS J, 2017,
284,
4328-4342.
[DOI no: ]
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PubMed id
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Abstract
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The Helicobacter pylori flagellum is a complex rotatory nanomachine fundamental
for the bacterium's survival in the human stomach. Protein FlgE is a component
of the hook, a flexible junction exposed on the cell surface. In the H. pylori
genome two different genes are present in different positions coding for
hypothetical FlgE. The first protein, FlgE1, is the actual component of the
flagellum hook, whilst the second, FlgE2, shares only 26% of the sequence
identity with the other and its physiological function is still undefined. We
have cloned, purified and crystallized FlgE2, whose structure, determined by the
single-wavelength anomalous diffraction method, shows that in overall
organization, the protein is composed of three distinct domains, two of them
relatively similar to those of FlgE from other Gram-negative bacteria, whilst
the third is peculiar to H. pylori. The crystal structure, along with the
detected interaction with the regulatory cap protein FlgD, suggests a
complementary function of FlgE1 and FlgE2 in the H. pylori flagellum, possibly
typical of polar flagella, confirming the role of both proteins in the flagellar
hook organization. Although some general features are shared with other
Gram-negative bacteria, the presence of two different hook proteins indicates
that the molecular organization of H. pylori flagellum has its own peculiarities.
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