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Structure paper

TitleStructural analysis of asparaginyl endopeptidase reveals the activation mechanism and a reversible intermediate maturation stage.
Journal, issue, pagesCell Res., Vol. 24, Page 344-358, Year 2014
Publish dateNov 19, 2013 (structure data deposition date)
AuthorsZhao, L. / Hua, T. / Crowley, C. / Ru, H. / Ni, X. / Shaw, N. / Jiao, L. / Ding, W. / Qu, L. / Hung, L.W. ...Zhao, L. / Hua, T. / Crowley, C. / Ru, H. / Ni, X. / Shaw, N. / Jiao, L. / Ding, W. / Qu, L. / Hung, L.W. / Huang, W. / Liu, L. / Ye, K. / Ouyang, S. / Cheng, G. / Liu, Z.J.
External linksCell Res. / PubMed:24407422
MethodsX-ray diffraction
Resolution2.006 - 2.8 Å
Structure data

PDB-4noj:
Crystal structure of the mature form of asparaginyl endopeptidase (AEP)/Legumain activated at pH 3.5
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-4nok:
Crystal structure of proenzyme asparaginyl endopeptidase (AEP)/Legumain at pH 7.5
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-4nol:
Crystal structure of proenzyme asparaginyl endopeptidase (AEP)/Legumain mutant D233A at pH 7.5
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-4nom:
Crystal structure of asparaginyl endopeptidase (AEP)/Legumain activated at pH 4.5
Method: X-RAY DIFFRACTION / Resolution: 2.006 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
KeywordsHYDROLASE / new fold / asparaginyl endopeptidase / substrate / extracellular

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