Stability data of FlgD from Helicobacter pylori and structural comparison with other homologs

Ivana Pulić; Laura Cendron; Marco Salamina; Patrizia Polverino de Laureto; Dubravka Matković-Čalogović; Giuseppe Zanotti

doi:10.1016/j.dib.2016.02.068

Stability data of FlgD from Helicobacter pylori and structural comparison with other homologs

Data Brief. 2016 Mar 4:7:493-501. doi: 10.1016/j.dib.2016.02.068. eCollection 2016 Jun.

Authors

Ivana Pulić¹, Laura Cendron², Marco Salamina³, Patrizia Polverino de Laureto⁴, Dubravka Matković-Čalogović⁵, Giuseppe Zanotti³

Affiliations

¹ University of Zagreb, Faculty of Science, Department of Chemistry, Division of General and Inorganic Chemistry, Horvatovac 102a, Zagreb 10000, Croatia; Department of Biomedical Sciences, University of Padua, Via Ugo Bassi 58/B, Padua 35131, Italy.
² Department of Biology, University of Padua, Via Ugo Bassi 58/B, Padua 35131, Italy.
³ Department of Biomedical Sciences, University of Padua, Via Ugo Bassi 58/B, Padua 35131, Italy.
⁴ Department of Pharmaceutical Sciences, University of Padua, Via Marzolo 5, Padua 35131, Italy.
⁵ University of Zagreb, Faculty of Science, Department of Chemistry, Division of General and Inorganic Chemistry, Horvatovac 102a, Zagreb 10000, Croatia.

Abstract

Flagellin component D (FlgD) from Helicobacter pylori is involved in the assembly of the hook of flagella, helical tubular structures that provide motility in non-filamentous bacteria. Data provided in this article refer to HpFlgD from strains 26695 (HpFlgD_26695) and G27 (HpFlgD_G27). Within this article, information on the secondary structure content and different type of interfaces found in the two crystal forms of HpFlgD (monoclinic, HpFlgD_m and tetragonal, HpFlgD_t) are provided, as well as the list of the hydrogen bonds between monomers that are relevant for their assembly into a tetramer. Additionally, data involving investigation of the size of HpFlgD in the solution and the crystallized HpFlgD are presented, "Crystal structure of truncated FlgD from the human pathogen Helicobacter pylori" [1]. The superposition of the different domains of HpFlgD (Fn-III and tudor domains) with the similar domains found in other species is shown, as well as the superposition of HpFlgD and modeled HpFlgE (flagellar hook protein).