4RTD

Escherichia coli alpha-2-macroglobulin activated by porcine elastase

4RTD の概要

• エントリーDOI: 10.2210/pdb4rtd/pdb
• 関連するPDBエントリー: 4ACQ 4U48 4U59
• 分子名称: Uncharacterized lipoprotein YfhM (1 entity in total)
• 機能のキーワード: thioester domain, macroglobulin, lipid binding protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell membrane ; Lipid-anchor : P76578
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 181618.08

構造登録者

Fyfe, C.D.,Grinter, R.,Roszak, A.W.,Josts, I.,Cogdell, R.J.,Walker, D. (登録日: 2014-11-14, 公開日: 2015-07-15, 最終更新日: 2024-11-20)

主引用文献

Fyfe, C.D.,Grinter, R.,Josts, I.,Mosbahi, K.,Roszak, A.W.,Cogdell, R.J.,Wall, D.M.,Burchmore, R.J.,Byron, O.,Walker, D.
Structure of protease-cleaved Escherichia coli alpha-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment.
Acta Crystallogr.,Sect.D, 71:1478-1486, 2015

PubMed Abstract: Bacterial α-2-macroglobulins have been suggested to function in defence as broad-spectrum inhibitors of host proteases that breach the outer membrane. Here, the X-ray structure of protease-cleaved Escherichia coli α-2-macroglobulin is described, which reveals a putative mechanism of activation and conformational change essential for protease inhibition. In this competitive mechanism, protease cleavage of the bait-region domain results in the untethering of an intrinsically disordered region of this domain which disrupts native interdomain interactions that maintain E. coli α-2-macroglobulin in the inactivated form. The resulting global conformational change results in entrapment of the protease and activation of the thioester bond that covalently links to the attacking protease. Owing to the similarity in structure and domain architecture of Escherichia coli α-2-macroglobulin and human α-2-macroglobulin, this protease-activation mechanism is likely to operate across the diverse members of this group.

PubMed: 26143919
DOI: 10.1107/S1399004715008548

実験手法

X-RAY DIFFRACTION (3.65 Å)