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Structure paper

TitleStructural analyses ofArabidopsis thalianalegumain gamma reveal differential recognition and processing of proteolysis and ligation substrates.
Journal, issue, pagesJ. Biol. Chem., Vol. 293, Page 8934-8946, Year 2018
Publish dateJun 29, 2017 (structure data deposition date)
AuthorsZauner, F.B. / Elsasser, B. / Dall, E. / Cabrele, C. / Brandstetter, H.
External linksJ. Biol. Chem. / PubMed:29628443
MethodsX-ray diffraction
Resolution1.5 Å
Structure data

PDB-5obt:
Fully activated A. thaliana legumain isoform gamma in complex with Ac-YVAD-CMK
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • arabidopsis thaliana (thale cress)
  • synthetic construct (others)
KeywordsHYDROLASE / Legumain / Asparaginyl endopeptidase / Vacuolar processing enzyme / peptide cyclase

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