Pulić Ivana, Cendron Laura, Salamina Marco, Polverino de Laureto Patrizia, Matković-Čalogović Dubravka, Zanotti Giuseppe
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.
Department of Biology, University of Padua, Via Ugo Bassi 58/B, Padua 35131, Italy.
Data Brief. 2016 Mar 4;7:493-501. doi: 10.1016/j.dib.2016.02.068. eCollection 2016 Jun.
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).
幽门螺杆菌的鞭毛蛋白组分D(FlgD)参与鞭毛钩的组装,鞭毛钩是一种螺旋管状结构,可赋予非丝状细菌运动能力。本文提供的数据涉及26695菌株(HpFlgD_26695)和G27菌株(HpFlgD_G27)的HpFlgD。本文提供了关于HpFlgD两种晶体形式(单斜晶系,HpFlgD_m和四方晶系,HpFlgD_t)的二级结构含量和不同类型界面的信息,以及单体之间与它们组装成四聚体相关的氢键列表。此外,还展示了涉及溶液中HpFlgD大小和结晶HpFlgD的研究数据,“人类病原体幽门螺杆菌截短型FlgD的晶体结构”[1]。展示了HpFlgD不同结构域(Fn-III和tudor结构域)与其他物种中相似结构域的叠加,以及HpFlgD与模拟的HpFlgE(鞭毛钩蛋白)的叠加。