Structure of a post-translationally processed heterodimeric double-headed Kunitz-type serineprotease inhibitor from potato

E.M. Meulenbroek, E.A.J. Thomassen, L.A.M. Pouvreau, J.P. Abrahams, H. Gruppen, N.S. Pannu

Research output: Contribution to journalArticleAcademicpeer-review

18 Citations (Scopus)

Abstract

Potato serine protease inhibitor (PSPI) constitutes about 22% of the total amount of proteins in potato tubers (cv. Elkana), making it the most abundant protease inhibitor in the plant. PSPI is a heterodimeric double-headed Kunitz-type serine protease inhibitor that can tightly and simultaneously bind two serine proteases by mimicking the substrate of the enzyme with its reactive-site loops. Here, the crystal structure of PSPI is reported, representing the first heterodimeric doubleheaded Kunitz-type serine protease inhibitor structure to be determined. PSPI has a-trefoil fold and, based on the structure, two reactive-site loops bearing residues Phe75 and Lys95 were identified.
Original languageEnglish
Pages (from-to)794-799
JournalActa Crystallographica Section D-Biological Crystallography
Volume68
Issue number7
DOIs
Publication statusPublished - 2012

Keywords

  • macromolecular crystallography
  • chymotrypsin inhibitor
  • molecular-replacement
  • proteinase-inhibitors
  • crystal-structure
  • reactive-site
  • cv elkana
  • refinement
  • seeds

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