1R19

Crystal Structure Analysis of S.epidermidis adhesin SdrG binding to Fibrinogen (Apo structure)

1R19 の概要

• エントリーDOI: 10.2210/pdb1r19/pdb
• 関連するPDBエントリー: 1R17
• 分子名称: fibrinogen-binding protein SdrG (1 entity in total)
• 機能のキーワード: mscramm, sdrg native, cell adhesion
• 由来する生物種: Staphylococcus epidermidis
• 細胞内の位置: Secreted, cell wall; Peptidoglycan-anchor (Potential): Q9KI13
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 154091.08

構造登録者

Ponnuraj, K.,Bowden, M.G.,Davis, S.,Gurusiddappa, S.,Moore, D.,Choe, D.,Xu, Y.,Hook, M.,Narayana, S.V.L. (登録日: 2003-09-23, 公開日: 2003-10-28, 最終更新日: 2023-08-23)

主引用文献

Ponnuraj, K.,Bowden, M.G.,Davis, S.,Gurusiddappa, S.,Moore, D.,Choe, D.,Xu, Y.,Hook, M.,Narayana, S.V.L.
A "dock, lock and latch" Structural Model for a Staphylococcal Adhesin Binding to Fibrinogen
Cell(Cambridge,Mass.), 115:217-228, 2003

PubMed Abstract: Gram-positive pathogens such as staphylococci contain multiple cell wall-anchored proteins that serve as an interface between the microbe and its environment. Some of these proteins act as adhesins and mediate bacterial attachment to host tissues. SdrG is a cell wall-anchored adhesin from Staphylococcus epidermidis that binds to the Bbeta chain of human fibrinogen (Fg) and is necessary and sufficient for bacterial attachment to Fg-coated biomaterials. Here, we present the crystal structures of the ligand binding region of SdrG as an apoprotein and in complex with a synthetic peptide analogous to its binding site in Fg. Analysis of the crystal structures, along with mutational studies of both the protein and of the peptide, reveals that SdrG binds to its ligand with a dynamic "dock, lock, and latch" mechanism. We propose that this mechanism represents a general mode of ligand binding for structurally related cell wall-anchored proteins of gram-positive bacteria.

PubMed: 14567919
DOI: 10.1016/S0092-8674(03)00809-2

実験手法

X-RAY DIFFRACTION (3.51 Å)