2GOM

Crystal structure of Efb-C from Staphylococcus aureus

2GOM の概要

• エントリーDOI: 10.2210/pdb2gom/pdb
• 関連するPDBエントリー: 2GOX
• 分子名称: Fibrinogen-binding protein (2 entities in total)
• 機能のキーワード: three-helix closed bundle with left-hand twist, cell adhesion-toxin complex, cell adhesion/toxin
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Secreted: P68798
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 14409.06

構造登録者

Hammel, M.,Geisbrecht, B.V. (登録日: 2006-04-13, 公開日: 2007-03-20, 最終更新日: 2024-02-14)

主引用文献

Hammel, M.,Sfyroera, G.,Ricklin, D.,Magotti, P.,Lambris, J.D.,Geisbrecht, B.V.
A structural basis for complement inhibition by Staphylococcus aureus.
Nat.Immunol., 8:430-437, 2007

PubMed Abstract: To provide insight into bacterial suppression of complement-mediated immunity, we present here structures of a bacterial complement inhibitory protein, both free and bound to its complement target. The 1.25-A structure of the complement component C3-inhibitory domain of Staphylococcus aureus extracellular fibrinogen-binding protein (Efb-C) demonstrated a helical motif involved in complement regulation, whereas the 2.2-A structure of Efb-C bound to the C3d domain of human C3 allowed insight into the recognition of complement proteins by invading pathogens. Our structure-function studies provided evidence for a previously unrecognized mode of complement inhibition whereby Efb-C binds to native C3 and alters the solution conformation of C3 in a way that renders it unable to participate in successful 'downstream' activation of the complement response.

PubMed: 17351618
DOI: 10.1038/ni1450

実験手法

X-RAY DIFFRACTION (1.25 Å)