Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp- containing aspartic proteinase from the flowers of Cynara cardunculus L.

Carlos Frazão, Isabel Bento, Júlia Costa, Cláudio M. Soares, Paula Veríssimo, Carlos Faro, Euclides Pires, Jon Cooper, Maria A. Carrondo

Research output: Contribution to journalArticlepeer-review

80 Citations (Scopus)

Abstract

Aspartic proteinases (AP) have been widely studied within the living world, but so far no plant AP have been structurally characterized. The refined cardosin A crystallographic structure includes two molecules, built up by two glycosylated peptide chains (31 and 15 kDa each). The fold of cardosin A is typical within the AP family. The giycosyl content is described by 19 sugar rings attached to Asn-67 and Asn-257. They are localized on the molecular surface away from the conserved active site and show a new glycan of the plant complex type. A hydrogen bond between Gln-126 and Manβ4 renders the monosaccharide oxygen O-2 sterically inaccessible to accept a xylosyl residue, therefore explaining the new type of the identified plant glycan. The Arg-Gly-Asp sequence, which has been shown to be involved in recognition of a putative cardosin A receptor, was found in a loop between two β-strands on the molecular surface opposite the active site cleft. Based on the crystal structure, a possible mechanism whereby cardosin A might be orientated at the cell surface of the style to interact with its putative receptor from pollen is proposed. The biological implications of these findings are also discussed.

Original languageEnglish
Pages (from-to)27694-27701
Number of pages8
JournalJournal of Biological Chemistry
Volume274
Issue number39
DOIs
Publication statusPublished - 24 Sep 1999

Keywords

  • aspartic proteinase
  • vegetable protein

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