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TitleThe macrocyclizing protease butelase 1 remains autocatalytic and reveals the structural basis for ligase activity.
Journal, issue, pagesPlant J., Vol. 98, Page 988-999, Year 2019
Publish dateMay 20, 2018 (structure data deposition date)
AuthorsJames, A.M. / Haywood, J. / Leroux, J. / Ignasiak, K. / Elliott, A.G. / Schmidberger, J.W. / Fisher, M.F. / Nonis, S.G. / Fenske, R. / Bond, C.S. / Mylne, J.S.
External linksPlant J. / PubMed:30790358
MethodsX-ray diffraction
Resolution3.1 Å
Structure data

PDB-6dhi:
Butelase 1: Auto-Catalytic Cleavage as an Evolutionary Constraint for Macrocyclizing Endopeptidases
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • clitoria ternatea (plant)
KeywordsPLANT PROTEIN / Hydrolase / Asparaginyl endopeptidase

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