FimDによる折りたたまれたタンパク質輸送の構造的およびエネルギー的基礎は,FimDによる折りたたまれたタンパク質輸送の構造的およびエネルギー的基礎である
Sebastian Geibel1, Erik Procko, Scott J Hultgren
1Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK.
Nature
|April 13, 2013
まとめ
尿病原性Escherichia coliは,宿主粘着のためにタイプ1 piliを使用します. この研究は,柱の延長複合体の構造を明らかにし,FimDの案内者が,形状の変化を通して柱の組立と分泌をどのように導くかを示しています.
科学分野:
- 微生物学 微生物学とは
- 構造生物学 構造生物学とは
- バイオケミストリー バイオケミストリー
背景:
- 1型ピリは,尿病原性Escherichia coliの重要な毒性因子であり,宿主組織粘着を媒介する.
- Pilus biogenesisは,FimDウッシャー,サブユニットポリメリゼーションと分泌を触媒化する外膜プラットフォームを含む.
- ピルスの生体生成の開始は理解されていますが,伸びのステップはほとんど特徴づけられていないままです.
研究 の 目的:
- 1型ピルス生物発生の延長段階を制御する構造的メカニズムを解明する.
- 柱の伸びと分泌を媒介するFimDウシャーの役割を調査する.
- 新生ピリがFimD孔を通してどのように転位するかを理解するために.
主な方法:
- 1型ピルス延長複合体の結晶構造の決定.
- FimDの構造分析は,柱の尖端構造と複雑な構造を導入しました.
- サブストラット-ウッシャー相互作用の生体物理的特徴.
主要な成果:
- 構造は,ピルス・バックスライディングを防ぐために不可欠なFimDアーサー内の構造変化を明らかにします.
- FimD孔とピルス基板の間の保存された円形の結合インターフェースは,ガイドされた輸送を容易にする.
- 座標孔の予期せぬ性質が特定され,効率的なピルス分泌に寄与しました.
結論:
- FimDウシャーは,特定の形状ダイナミクスと孔-ウシャーの相互作用を使用して,片方向のピルス延長を確保します.
- 伸縮複合体の構造的な洞察は,ピルス分泌のメカニズム的理解を提供します.
- この研究は,バクテリアの粘着メカニズムと潜在的な治療標的に関する私たちの知識を前進させます.
関連する概念動画
Protein Folding
Overview
Protein Folding
Overview
Molecular Chaperones and Protein Folding
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
Energy to Drive Translocation
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Generally, polypeptides are unfolded by two distinct...
Protein Folding
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Molecular Chaperones and Protein Folding
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...


