2enr

File:2enr.gif

spinqualitylabelsall models 2enr, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CO-CRYSTALS OF DEMETALLIZED CONCANAVALIN A WITH CADMIUM HAVING A CADMIUM ION BOUND IN BOTH THE S1 SITE AND THE S2 SITE

OverviewOverview

The crystal structures of cadmium/cadmium and zinc/calcium concanavalin A, (con A) at pH 5.0 and pH 6.15, respectively, were determined. The, structure of cadmium/cadmium con A confirms that the secondary, Cd(2+)-binding site S3 is empty at pH 5. The metal-binding sites S1 and S2, are only very slightly affected by the substitution with cadmium. On the, other hand, S1 and S2 and most of the protein surface of zinc/calcium con, A at pH 6.15 differ from other fully metal-bound and carbohydrate-free, structures. Most of these structural differences at the protein surface, are a result of the interplay between metal binding, protonation and, crystal packing. This interplay is expressed by relative rotations and, translations of the con A units in alternative crystal packings and, participation in space-group conversions inside crystals in situ. The, particular crystal packing of zinc/calcium con A creates a novel, zinc-binding site S4. The Zn(2+) ion in S4 ligates two aspartates from one, tetramer and a histidine from a symmetry-related tetramer.

About this StructureAbout this Structure

2ENR is a Single protein structure of sequence from Canavalia ensiformis with CD as ligand. Structure known Active Sites: S1 and S2. Full crystallographic information is available from OCA.

ReferenceReference

Zinc/calcium- and cadmium/cadmium-substituted concanavalin A: interplay of metal binding, pH and molecular packing., Bouckaert J, Loris R, Wyns L, Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1569-76. PMID:11092923

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