2enr: Difference between revisions
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==Overview== | ==Overview== | ||
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, . | 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 Structure== | ==About this Structure== | ||
2ENR is a | 2ENR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Sites: S1 and S2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ENR OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: plant lectin]] | [[Category: plant lectin]] | ||
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Revision as of 13:19, 5 November 2007
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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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