3QZ0

Structure of Treponema denticola Factor H Binding protein (FhbB), selenomethionine derivative

3QZ0 の概要

• エントリーDOI: 10.2210/pdb3qz0/pdb
• 分子名称: Factor H binding protein, THIOCYANATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: factor h binding protein, factor h, protein binding
• 由来する生物種: Treponema denticola
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21609.98

構造登録者

Miller, D.P.,McDowell, J.V.,Heroux, A.,Bell, J.K.,Marconi, R.T.,Conrad, D.H.,Burgner, J.W. (登録日: 2011-03-04, 公開日: 2012-03-07, 最終更新日: 2024-11-20)

主引用文献

Miller, D.P.,Bell, J.K.,McDowell, J.V.,Conrad, D.H.,Burgner, J.W.,Heroux, A.,Marconi, R.T.
Structure of factor H-binding protein B (FhbB) of the periopathogen, Treponema denticola: insights into progression of periodontal disease.
J.Biol.Chem., 287:12715-12722, 2012

PubMed Abstract: Periodontitis is the most common disease of microbial etiology in humans. Periopathogen survival is dependent upon evasion of complement-mediated destruction. Treponema denticola, an important contributor to periodontitis, evades killing by the alternative complement cascade by binding factor H (FH) to its surface. Bound FH is rapidly cleaved by the T. denticola protease, dentilisin. In this report, the structure of the T. denticola FH-binding protein, FhbB, was solved to 1.7 Å resolution. FhbB possesses a unique fold that imparts high thermostability. The kinetics of the FH/FhbB interaction were assessed using surface plasmon resonance. A K(D) value in the micromolar range (low affinity) was demonstrated, and rapid off kinetics were observed. Site-directed mutagenesis and sucrose octasulfate competition assays collectively indicate that the negatively charged face of FhbB binds within FH complement control protein module 7. This study provides significant new insight into the molecular basis of FH/FhbB interaction and advances our understanding of the role that T. denticola plays in the development and progression of periodontal disease.

PubMed: 22371503
DOI: 10.1074/jbc.M112.339721

実験手法

X-RAY DIFFRACTION (1.77 Å)