Structure of protease-cleaved Escherichia coli[alpha]-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 71; no. 7; p. 1478
• Main Authors: Fyfe, Cameron D, Grinter, Rhys, Josts, Inokentijs, Mosbahi, Khedidja, Roszak, Aleksander W, Cogdell, Richard J, Wall, Daniel M, Burchmore, Richard J S, Byron, Olwyn, Walker, Daniel
• Format: Journal Article
• Language: English
• Published: Chester Wiley Subscription Services, Inc 01.07.2015
• Subjects: Bacteriology; E coli

Bacterial [alpha]-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[alpha]-2-macroglobulin is described, which reveals a putative mechanism of activ...