1b5f

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[[Image:1b5f.gif|left|200px]]
[[Image:1b5f.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1b5f", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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{{STRUCTURE_1b5f| PDB=1b5f | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5f OCA], [http://www.ebi.ac.uk/pdbsum/1b5f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b5f RCSB]</span>
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'''NATIVE CARDOSIN A FROM CYNARA CARDUNCULUS L.'''
'''NATIVE CARDOSIN A FROM CYNARA CARDUNCULUS L.'''
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[[Category: Carrondo, M A.]]
[[Category: Carrondo, M A.]]
[[Category: Frazao, C.]]
[[Category: Frazao, C.]]
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[[Category: hydrolase(aspartic proteinase),]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:05:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:53:57 2008''
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Revision as of 08:05, 2 May 2008

Image:1b5f.gif

Template:STRUCTURE 1b5f

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 Fri May 2 11:05:47 2008

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