1b5f
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1b5f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b5f, resolution 1.72Å" /> '''NATIVE CARDOSIN A FR...)
Next diff →
Revision as of 21:37, 24 November 2007
|
NATIVE CARDOSIN A FROM CYNARA CARDUNCULUS L.
Overview
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.
About this Structure
1B5F is a Single protein structure of sequence from Cynara cardunculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp-containing aspartic proteinase from the flowers of Cynara cardunculus L., Frazao C, Bento I, Costa J, Soares CM, Verissimo P, Faro C, Pires E, Cooper J, Carrondo MA, J Biol Chem. 1999 Sep 24;274(39):27694-701. PMID:10488111
Page seeded by OCA on Sat Nov 24 23:44:49 2007
