2enr

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[[Image:2enr.jpg|left|200px]]<br /><applet load="2enr" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2enr.jpg|left|200px]]
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caption="2enr, resolution 2.35&Aring;" />
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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'''<br />
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{{Structure
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|PDB= 2enr |SIZE=350|CAPTION= <scene name='initialview01'>2enr</scene>, resolution 2.35&Aring;
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|SITE= <scene name='pdbsite=S1:Transition+Metal+Binding+Site+S1+6-Coordinated+Octahedra+...'>S1</scene> and <scene name='pdbsite=S2:Ca+Binding+Site+S2+7-Coordinated+Distorted+Octahedral+Co+...'>S2</scene>
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|LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene>
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|ACTIVITY=
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|GENE=
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}}
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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'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=S1:Transition+Metal+Binding+Site+S1+6-Coordinated+Octahedra+...'>S1</scene> and <scene name='pdbsite=S2:Ca+Binding+Site+S2+7-Coordinated+Distorted+Octahedral+Co+...'>S2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ENR OCA].
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2ENR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ENR OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11092923 11092923]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11092923 11092923]
[[Category: Canavalia ensiformis]]
[[Category: Canavalia ensiformis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: cadmium]]
[[Category: cadmium]]
[[Category: carbohydrate binding]]
[[Category: carbohydrate binding]]
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[[Category: concanavalin a]]
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[[Category: concanavalin some]]
[[Category: metal binding]]
[[Category: metal binding]]
[[Category: plant lectin]]
[[Category: plant lectin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:12:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:42:27 2008''

Revision as of 14:42, 20 March 2008


PDB ID 2enr

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, resolution 2.35Å
Sites: and
Ligands:
Coordinates: save as pdb, mmCIF, xml



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


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

2ENR is a Single protein structure of sequence from Canavalia ensiformis. 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

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