Stability data of FlgD from Helicobacter pylori Q2 and structural comparison with other homologs
Ivana Pulic, Laura Cendron, Marco Salamina, Patrizia Polverino de Laureto, Dubravka Matković-Čalogović, Giuseppe Zanotti
Data in Brief
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” . The superposition of the different domains ofHpFlgD (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).
Circular dichroism, Secondary structure, Biochemistry