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| - | [[Image:1apn.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1apn| PDB=1apn | SCENE= }} | | {{STRUCTURE_1apn| PDB=1apn | SCENE= }} |
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| - | '''THE CRYSTALLOGRAPHIC STRUCTURE OF METAL-FREE CONCANAVALIN A AT 2.5 ANGSTROMS RESOLUTION'''
| + | ===THE CRYSTALLOGRAPHIC STRUCTURE OF METAL-FREE CONCANAVALIN A AT 2.5 ANGSTROMS RESOLUTION=== |
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| - | ==Overview==
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| - | The three-dimensional structure of demetallized concanavalin A has been determined at 2.5 A resolution and refined to a crystallographic R-factor of 18%. The lectin activity of concanavalin A requires the binding of both a transition metal ion, generally Mn2+, and a Ca2+ ion in two neighboring sites in close proximity to the carbohydrate binding site. Large structural differences between the native and the metal-free lectin are observed in the metal-binding region and consequently for the residues involved in the specific binding of saccharides. The demetallization invokes a series of conformational changes in the protein backbone, apparently initiated mainly by the loss of the calcium ion. Most of the Mn2+ ligands retain their position, but the Ca2+ binding site is destroyed. The Ala207-Asp208 peptide bond, in the beta-strand neighboring the metal-binding sites, undergoes a cis to trans isomerization. The cis conformation for this bond is a highly conserved feature among the leguminous lectins and is critically maintained by the Ca2+ ion in metal-bound concanavalin A. A further and major change adjacent to the isomerized bond is an expansion of the loop containing the monosaccharide ligand residues Leu99 and Tyr100. The dispersion of the ligand residues for the monosaccharide binding site (Asn14, Agr228, Asp208, Leu99, and Tyr100) in metal-free concanavalin A abolishes the lectin's ability to bind saccharides. Since the quaternary structure of legume lectins is essential to their biological role, the tetramer formation was analyzed. In the crystal (pH 5), the metal-free concanavalin A dimers associate into a tetramer that is similar to the native one, but with a drastically reduced number of inter-dimer interactions. This explains the tetramer dissociation into dimers below pH values of 6.5.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8749847}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8749847 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8749847}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Wyns, L.]] | | [[Category: Wyns, L.]] |
| | [[Category: Lectin]] | | [[Category: Lectin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:33:18 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:21:52 2008'' |
Revision as of 14:21, 30 June 2008
Template:STRUCTURE 1apn
THE CRYSTALLOGRAPHIC STRUCTURE OF METAL-FREE CONCANAVALIN A AT 2.5 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 8749847
About this Structure
1APN is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.
Reference
Crystallographic structure of metal-free concanavalin A at 2.5 A resolution., Bouckaert J, Loris R, Poortmans F, Wyns L, Proteins. 1995 Dec;23(4):510-24. PMID:8749847
Page seeded by OCA on Mon Jun 30 17:21:52 2008
