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Structure paper

TitleStructural and time-resolved mechanistic investigations of protein hydrolysis by the acidic proline-specific endoprotease from Aspergillus niger.
Journal, issue, pagesProtein Sci., Vol. 33, Page e4856-e4856, Year 2024
Publish dateSep 22, 2022 (structure data deposition date)
AuthorsPijning, T. / Vujicic-Zagar, A. / van der Laan, J.M. / de Jong, R.M. / Ramirez-Palacios, C. / Vente, A. / Edens, L. / Dijkstra, B.W.
External linksProtein Sci. / PubMed:38059672
MethodsX-ray diffraction
Resolution2.42 - 2.7 Å
Structure data

PDB-8b57:
Structure of prolyl endoprotease from Aspergillus niger CBS 109712
Method: X-RAY DIFFRACTION / Resolution: 2.42 Å

PDB-8bbx:
Structure of prolyl endoprotease from Aspergillus niger CBS 109712 in space group C222(1)
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-GOL:
GLYCEROL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

Source
  • aspergillus niger (mold)
KeywordsHYDROLASE / Endoprotease / proline-specific / S28 peptidase

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