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| {{STRUCTURE_3enr| PDB=3enr | SCENE= }} | | {{STRUCTURE_3enr| PDB=3enr | SCENE= }} |
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| '''ZINC-CALCIUM CONCANAVALIN A AT PH 6.15'''
| | ===ZINC-CALCIUM CONCANAVALIN A AT PH 6.15=== |
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| ==Overview==
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| 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 line below this paragraph, {{ABSTRACT_PUBMED_11092923}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11092923 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11092923}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Metal binding]] | | [[Category: Metal binding]] |
| [[Category: Ph]] | | [[Category: Ph]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:00:52 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:33:15 2008'' |
