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TitleStructure of protease-cleaved Escherichia coli alpha-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 71, Page 1478-1486, Year 2015
Publish dateNov 14, 2014 (structure data deposition date)
AuthorsFyfe, C.D. / Grinter, R. / Josts, I. / Mosbahi, K. / Roszak, A.W. / Cogdell, R.J. / Wall, D.M. / Burchmore, R.J. / Byron, O. / Walker, D.
External linksActa Crystallogr. ,Sect. D / PubMed:26143919
MethodsX-ray diffraction
Resolution3.65 Å
Structure data

PDB-4rtd:
Escherichia coli alpha-2-macroglobulin activated by porcine elastase
Method: X-RAY DIFFRACTION / Resolution: 3.65 Å

Source
  • escherichia coli (E. coli)
KeywordsLIPID BINDING PROTEIN / thioester domain / macroglobulin

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