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Croatica Chemica Acta, Vol. 89 No. 2, 2016.

Izvorni znanstveni članak

https://doi.org/10.5562/cca2942

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

Ivana Kekez orcid id orcid.org/0000-0001-8690-5465 ; University of Zagreb, Faculty of Science, Department of Chemistry, Division of General and Inorganic Chemistry, Horvatovac 102a, Zagreb, HR-10000, Croatia
Laura Cendron orcid id orcid.org/0000-0002-0125-0461 ; Department of Biology, University of Padua, Via Ugo Bassi 58/B, Padua, IT-35131, Italy
Mario Stojanović orcid id orcid.org/0000-0002-6687-1808 ; University of Zagreb, Faculty of Science, Department of Chemistry, Division of General and Inorganic Chemistry, Horvatovac 102a, Zagreb, HR-10000, Croatia
Giuseppe Zanotti ; Department of Biomedical Sciences, University of Padua, Via Ugo Bassi 58/B, Padua, IT-35131, Italy
Dubravka Matković-Čalogović orcid id orcid.org/0000-0003-4909-8312 ; University of Zagreb, Faculty of Science, Department of Chemistry, Division of General and Inorganic Chemistry, Horvatovac 102a, Zagreb, HR-10000, Croatia

Puni tekst: engleski pdf 5.345 Kb

str. 229-235

preuzimanja: 1.609

citiraj

Sažetak

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.

This work is licensed under a Creative Commons Attribution 4.0 International License.

Ključne riječi

<i>Helicobacter pylori</i>; strain 26695; FlgD; stability; monoclinic crystal structure

Hrčak ID:

166011

URI

https://hrcak.srce.hr/166011

Datum izdavanja:

21.6.2016.

Posjeta: 2.494 *