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Pregled bibliografske jedinice broj: 920693

Structural characterization of FlgE2 protein from Helicobacter pylori hook


Loconte, Valentina; Kekez, Ivana; Matković-Čalogović, Dubravka; Zanotti, Giuseppe
Structural characterization of FlgE2 protein from Helicobacter pylori hook // The FEBS journal, 284 (2017), 24; 4328-4342 doi:10.1111/febs.14312 (podatak o recenziji nije dostupan, članak, znanstveni)


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Naslov
Structural characterization of FlgE2 protein from Helicobacter pylori hook

Autori
Loconte, Valentina ; Kekez, Ivana ; Matković-Čalogović, Dubravka ; Zanotti, Giuseppe

Izvornik
The FEBS journal (1742-464X) 284 (2017), 24; 4328-4342

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
crystal structure ; flagella ; Helicobacter pylori ; hook ; host–pathogen interaction

Sažetak
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.

Izvorni jezik
Engleski

Znanstvena područja
Kemija



POVEZANOST RADA


Ustanove:
Prirodoslovno-matematički fakultet, Zagreb

Poveznice na cjeloviti tekst rada:

doi doi.org febs.onlinelibrary.wiley.com

Citiraj ovu publikaciju:

Loconte, Valentina; Kekez, Ivana; Matković-Čalogović, Dubravka; Zanotti, Giuseppe
Structural characterization of FlgE2 protein from Helicobacter pylori hook // The FEBS journal, 284 (2017), 24; 4328-4342 doi:10.1111/febs.14312 (podatak o recenziji nije dostupan, članak, znanstveni)
Loconte, V., Kekez, I., Matković-Čalogović, D. & Zanotti, G. (2017) Structural characterization of FlgE2 protein from Helicobacter pylori hook. The FEBS journal, 284 (24), 4328-4342 doi:10.1111/febs.14312.
@article{article, author = {Loconte, Valentina and Kekez, Ivana and Matkovi\'{c}-\v{C}alogovi\'{c}, Dubravka and Zanotti, Giuseppe}, year = {2017}, pages = {4328-4342}, DOI = {10.1111/febs.14312}, keywords = {crystal structure, flagella, Helicobacter pylori, hook, host–pathogen interaction}, journal = {The FEBS journal}, doi = {10.1111/febs.14312}, volume = {284}, number = {24}, issn = {1742-464X}, title = {Structural characterization of FlgE2 protein from Helicobacter pylori hook}, keyword = {crystal structure, flagella, Helicobacter pylori, hook, host–pathogen interaction} }
@article{article, author = {Loconte, Valentina and Kekez, Ivana and Matkovi\'{c}-\v{C}alogovi\'{c}, Dubravka and Zanotti, Giuseppe}, year = {2017}, pages = {4328-4342}, DOI = {10.1111/febs.14312}, keywords = {crystal structure, flagella, Helicobacter pylori, hook, host–pathogen interaction}, journal = {The FEBS journal}, doi = {10.1111/febs.14312}, volume = {284}, number = {24}, issn = {1742-464X}, title = {Structural characterization of FlgE2 protein from Helicobacter pylori hook}, keyword = {crystal structure, flagella, Helicobacter pylori, hook, host–pathogen interaction} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


Citati:





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