4BOD

Complement regulator acquiring outer surface protein BbCRASP-4 or ErpC from Borrelia burgdorferi

4BOD の概要

• エントリーDOI: 10.2210/pdb4bod/pdb
• 関連するPDBエントリー: 4BOB
• 分子名称: ERPC (1 entity in total)
• 機能のキーワード: cell adhesion, lipoprotein, complement factors, outer surface lipoprotein, 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: 34970.79

構造登録者

Brangulis, K.,Petrovskis, I.,Kazaks, A.,Baumanis, V.,Tars, K. (登録日: 2013-05-18, 公開日: 2014-05-28, 最終更新日: 2023-12-20)

主引用文献

Brangulis, K.,Petrovskis, I.,Kazaks, A.,Akopjana, I.,Tars, K.
Crystal Structures of the Erp Protein Family Members Erpp and Erpc from Borrelia Burgdorferi Reveal the Reason for Different Affinities for Complement Regulator Factor H.
Biochim.Biophys.Acta, 1854:349-, 2015

PubMed Abstract: Borrelia burgdorferi is the causative agent of Lyme disease, which can be acquired after the bite of an infected Ixodes tick. As a strategy to resist the innate immunity and to successfully spread and proliferate, B. burgdorferi expresses a set of outer membrane proteins that are capable of binding complement regulator factor H (CFH), factor H-like protein 1 (CFHL-1) and factor H-related proteins (CFHR) to avoid complement-mediated killing. B. burgdorferi B31 contains three proteins that belong to the Erp (OspE/F-related) protein family and are capable of binding CFH and some CFHRs, namely ErpA, ErpC and ErpP. We have determined the crystal structure of ErpP at 2.53Å resolution and the crystal structure of ErpC at 2.15Å resolution. Recently, the crystal structure of the Erp family member OspE from B. burgdorferi N40 was determined in complex with CFH domains 19-20, revealing the residues involved in the complex formation. Despite the high sequence conservation between ErpA, ErpC, ErpP and the homologous protein OspE (78-80%), the affinity for CFH and CFHRs differs markedly among the Erp family members, suggesting that ErpC may bind only CFHRs but not CFH. A comparison of the binding site in OspE with those of ErpC and ErpP revealed that the extended loop region, which is only observed in the potential binding site of ErpC, plays an important role by preventing the binding of CFH. These results can explain the inability of ErpC to bind CFH, whereas ErpP and ErpA still possess the ability to bind CFH.

PubMed: 25582082
DOI: 10.1016/J.BBAPAP.2014.12.025

実験手法

X-RAY DIFFRACTION (3.15 Å)