3enr
From Proteopedia
(New page: 200px<br /><applet load="3enr" size="450" color="white" frame="true" align="right" spinBox="true" caption="3enr, resolution 2.4Å" /> '''ZINC-CALCIUM CONCANAV...) |
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| - | [[Image:3enr.jpg|left|200px]]<br /><applet load="3enr" size=" | + | [[Image:3enr.jpg|left|200px]]<br /><applet load="3enr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="3enr, resolution 2.4Å" /> | caption="3enr, resolution 2.4Å" /> | ||
'''ZINC-CALCIUM CONCANAVALIN A AT PH 6.15'''<br /> | '''ZINC-CALCIUM CONCANAVALIN A AT PH 6.15'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structures of cadmium/cadmium and zinc/calcium concanavalin A | + | 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== | ||
| - | 3ENR 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 ZN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 3ENR 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 <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ENR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ph]] | [[Category: ph]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:09:09 2008'' |
Revision as of 17:09, 21 February 2008
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ZINC-CALCIUM CONCANAVALIN A AT PH 6.15
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.
About this Structure
3ENR is a Single protein structure of sequence from Canavalia ensiformis with and as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 19:09:09 2008
Categories: Canavalia ensiformis | Single protein | Bouckaert, J. | Loris, R. | Wyns, L. | CA | ZN | Concanavalin a | Lectin | Metal binding | Ph
