6ROC

Crystal structure of Borrelia burgdorferi outer surface protein BBA69, mutant Leu214Met (Se-Met data)

6ROC の概要

• エントリーDOI: 10.2210/pdb6roc/pdb
• 分子名称: Putative surface protein (1 entity in total)
• 機能のキーワード: outer surface protein, pfam54, membrane protein
• 由来する生物種: Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44938.97

構造登録者

Brangulis, K.,Akopjana, I.,Petrovskis, I.,Kazaks, A.,Tars, K. (登録日: 2019-05-11, 公開日: 2019-06-26, 最終更新日: 2024-05-15)

主引用文献

Brangulis, K.,Akopjana, I.,Petrovskis, I.,Kazaks, A.,Tars, K.
Crystal structure of Borrelia burgdorferi outer surface protein BBA69 in comparison to the paralogous protein CspA.
Ticks Tick Borne Dis, 10:1135-1141, 2019

PubMed Abstract: The spirochete Borrelia burgdorferi sensu lato is the causative agent of Lyme borreliosis - the most common tick-borne disease in Europe and the United States. Spirochetes are transmitted from infected Ixodes ticks to the mammalian host when the ticks feed. In general, the transfer process of the borreliae is quite complicated, as the environments in the tick and the new mammalian host differs significantly. Therefore, Borrelia changes the expression profile of dozens of proteins, mainly outer surface proteins, to adapt to the new tasks and needs in the new organism. In the transfer process from the tick to the mammalian host, spirochetes that cause Lyme disease show the strongest upregulation of members of paralogous gene family 54 (PFam54). PFam54 members encode 10 proteins, and BBA69 is one of its members. Although several PFam54 members play an important role in the pathogenesis of Lyme disease, the exact function has been determined only for CspA, which binds complement regulator factor H (CFH) and factor H-like protein 1 (FHL-1); thus, CspA is essential to resist the vertebrate host's immune response. In the current study, we determined the crystal structure of BBA69 at a 2.25 Ǻ resolution. The BBA69 structure revealed a seven α-helical BbCRASP-1 fold previously found only in PFam54 member proteins. Among the PFam54 members, BBA69 shares the highest sequence identity (61%) and 3-D similarity with CspA. Although none of the PFam54 members besides CspA bind CFH and FHL-1, in the current study, we investigated the structural differences accounting for the divergence in the functions of these proteins. The results clearly indicated that the C-terminal α-helix is the main determinant of this functional divergence. The results provide better insight into the PFam54 proteins that play an important role in the pathogenesis of Lyme disease.

PubMed: 31204045
DOI: 10.1016/j.ttbdis.2019.06.009

実験手法

X-RAY DIFFRACTION (2.9 Å)