2enr: Difference between revisions

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==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, 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.

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==

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[[Category: plant lectin]]

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@@ Line 4: / Line 4: @@
 ==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, 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.
+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==
@@ Line 23: / Line 23: @@
 [[Category: plant lectin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:37:46 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:12:54 2008''