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

Fyfe, C.D.; Grinter, R.; Josts, I.; Mosbahi, K.; Roszak, A.W.; Cogdell, R.J.; Wall, D.M.; Burchmore, R.J.S.; Byron, O.; Walker, D.

doi:10.1107/S1399004715008548

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 4
Conformational shift of the TED and thioester of protease-activated ECAM. (a) Superposition of protease-cleaved ECAM (red) and SaA2M (blue) showing a 36 Å shift of the TED. Structures were overlaid by superposition of MG8 containing the BRD. (b) Overlaid elastase-cleaved ECAM (red) and native SaA2M (blue) TEDs. Tyrosines thought to protect the thioester region from hydrolysis in native SaA2M (Tyr1175 and Tyr1177) are orientated away from the protease-activated ECAM thioester region (Tyr1183 and Tyr1185 in protease-activated ECAM).

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 71| Part 7| June 2015| Pages 1478-1486

doi:10.1107/S1399004715008548

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