4D53

Outer surface protein BB0689 from Borrelia burgdorferi

4D53 の概要

• エントリーDOI: 10.2210/pdb4d53/pdb
• 分子名称: BB0689 (2 entities in total)
• 機能のキーワード: structural protein, lipoprotein, cap domain, lyme disease
• 由来する生物種: BORRELIA BURGDORFERI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31832.55

構造登録者

Brangulis, K.,Petrovskis, I.,Kazaks, A.,Tars, K. (登録日: 2014-11-02, 公開日: 2015-10-14, 最終更新日: 2024-05-08)

主引用文献

Brangulis, K.,Jaudzems, K.,Petrovskis, I.,Akopjana, I.,Kazaks, A.,Tars, K.
Structural and Functional Analysis of Bb0689 from Borrelia Burgdorferi, a Member of the Bacterial CAP Superfamily.
J.Struct.Biol., 192:320-, 2015

PubMed Abstract: Spirochete Borrelia burgdorferi is the causative agent of Lyme disease and is transmitted from infected Ixodes ticks to a mammalian host after a tick bite. The outer surface protein BB0689 from B. burgdorferi is up-regulated when the tick feeds, which indicates a potential role for BB0689 in Lyme disease pathogenesis. We have determined the crystal structure of BB0689, which revealed that the protein belongs to the CAP superfamily. Though the CAP domain is widespread in all three cellular domains of life, thus far the CAP domain has been studied only in eukaryotes, in which it is usually linked to certain other domains to form a multi-domain protein and is associated with the mammalian reproductive tract, the plant response to pathogens, venom allergens from insects and reptiles, and the growth of human brain tumors. Though the exact function of the isolated CAP domain remains ambiguous, several functions, including the binding of cholesterol, lipids and heparan sulfate, have been recently attributed to different CAP domain proteins. In this study, the bacterial CAP domain structure was analyzed and compared with the previously solved crystal structures of representative CAPs, and the function of BB0689 was examined. To determine the potential function of BB0689 and ascertain whether the functions that have been attributed to the CAP domain proteins are conserved, the binding of previously reported CAP domain interaction partners was analyzed, and the results suggested that BB0689 has a unique function that is yet to be discovered.

PubMed: 26407658
DOI: 10.1016/J.JSB.2015.09.007

実験手法

X-RAY DIFFRACTION (1.85 Å)