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Literature summary for 3.4.23.40 extracted from

  • Frazao, C.; Bento, I.; Costa, J.; Soares, C.M.; Verissimo, P.; Faro, C.; Pires, E.; Cooper, J.; Carrondo, M.A.
    Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp-containing aspartic proteinase from the flowers of Cynara cardunculus L. (1999), J. Biol. Chem., 274, 27694-27701.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
to 1.72 A resoultion. Structure includes two molecules, built up by two glycosylated peptide chains of 31 and 15 kDa. The glycosyl content is described by 19 sugar rings attached to residues Asn67 and Asn257 localized on the molecular surface away from the conserved active site. A hydrogen bond between Gln126 and Manbeta4 renders the monosaccharide oxygen O2 sterically inaccessible to accept a xylosyl residue, explaining a hitherto unknown type of plant glycan. The Arg-Gly-Asp sequence, involved in recognition of a putative cardosin A receptor, is found in a loop between two beta-strands on the molecular surface opposite the active site cleft Cynara cardunculus

Organism

Organism UniProt Comment Textmining
Cynara cardunculus Q9XFX3
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein structure contains two glycosylated peptide chains of 31 and 15 kDa. 19 sugar rings are attached to residues Asn67 and Asn257 localized on the molecular surface away from the conserved active site Cynara cardunculus

Source Tissue

Source Tissue Comment Organism Textmining