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
Affiliations
Ivana Pulić
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
Laura Cendron
Department of Biology, University of Padua, Via Ugo Bassi 58/B, Padua 35131, Italy
Marco Salamina
Department of Biomedical Sciences, University of Padua, Via Ugo Bassi 58/B, Padua 35131, Italy
Patrizia Polverino de Laureto
Department of Pharmaceutical Sciences, University of Padua, Via Marzolo 5, Padua 35131, Italy
Dubravka Matković-Čalogović
University of Zagreb, Faculty of Science, Department of Chemistry, Division of General and Inorganic Chemistry, Horvatovac 102a, Zagreb 10000, Croatia; Corresponding author at: University of Zagreb, Faculty of Science, Department of Chemistry, Division of General and Inorganic Chemistry, Horvatovac 102a, Zagreb 10000, Croatia, Tel.: +38514606345.
Giuseppe Zanotti
Department of Biomedical Sciences, University of Padua, Via Ugo Bassi 58/B, Padua 35131, Italy; Corresponding author at: Department of Biomedical Sciences, University of Padua, Via U. Bassi 58/B, Padua 35131, Italy. Tel.: ++39 0498276409.
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).
