1B5F
NATIVE CARDOSIN A FROM CYNARA CARDUNCULUS L.
Summary for 1B5F
| Entry DOI | 10.2210/pdb1b5f/pdb |
| Descriptor | PROTEIN (CARDOSIN A), alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | hydrolase, aspartic proteinase |
| Biological source | Cynara cardunculus More |
| Total number of polymer chains | 4 |
| Total formula weight | 74386.40 |
| Authors | Frazao, C.,Bento, I.,Carrondo, M.A. (deposition date: 1999-01-06, release date: 1999-01-13, Last modification date: 2024-10-30) |
| Primary citation | 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. J.Biol.Chem., 274:27694-27701, 1999 Cited by PubMed 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 glycosyl 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 Manbeta4 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 beta-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. PubMed: 10488111DOI: 10.1074/jbc.274.39.27694 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.72 Å) |
Structure validation
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