1ier

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[[Image:1ier.gif|left|200px]]<br /><applet load="1ier" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ier.gif|left|200px]]
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caption="1ier, resolution 2.26&Aring;" />
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'''CUBIC CRYSTAL STRUCTURE OF NATIVE HORSE SPLEEN FERRITIN'''<br />
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{{Structure
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|PDB= 1ier |SIZE=350|CAPTION= <scene name='initialview01'>1ier</scene>, resolution 2.26&Aring;
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|SITE= <scene name='pdbsite=1:Metal-Binding+Site.+Site+1+Is+Exposed+To+The+Exterior+Of+...'>1</scene>, <scene name='pdbsite=2:Metal+Site.+Site+2+Is+Located+Near+The+Inner+Surface+Of+...'>2</scene> and <scene name='pdbsite=3:Metal-Binding+Site+Cd+203+Is+Located+On+A+Two-Fold+Axis+...'>3</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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'''CUBIC CRYSTAL STRUCTURE OF NATIVE HORSE SPLEEN FERRITIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1IER is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=1:Metal-Binding+Site.+Site+1+Is+Exposed+To+The+Exterior+Of+...'>1</scene>, <scene name='pdbsite=2:Metal+Site.+Site+2+Is+Located+Near+The+Inner+Surface+Of+...'>2</scene> and <scene name='pdbsite=3:Metal-Binding+Site+Cd+203+Is+Located+On+A+Two-Fold+Axis+...'>3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IER OCA].
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1IER is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IER OCA].
==Reference==
==Reference==
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Comparison of the structures of the cubic and tetragonal forms of horse-spleen apoferritin., Granier T, Gallois B, Dautant A, Langlois d'Estaintot B, Precigoux G, Acta Crystallogr D Biol Crystallogr. 1997 Sep 1;53(Pt 5):580-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299889 15299889]
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Comparison of the structures of the cubic and tetragonal forms of horse-spleen apoferritin., Granier T, Gallois B, Dautant A, Langlois d'Estaintot B, Precigoux G, Acta Crystallogr D Biol Crystallogr. 1997 Sep 1;53(Pt 5):580-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299889 15299889]
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: iron storage]]
[[Category: iron storage]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:49:26 2008''

Revision as of 09:49, 20 March 2008


PDB ID 1ier

Drag the structure with the mouse to rotate
, resolution 2.26Å
Sites: , and
Ligands:
Coordinates: save as pdb, mmCIF, xml



CUBIC CRYSTAL STRUCTURE OF NATIVE HORSE SPLEEN FERRITIN


Overview

Horse-spleen apoferritin is known to crystallize in three different space groups, cubic F432, tetragonal P42(1)2 and orthorhombic P2(1)2(1)2. A structure comparison of the cubic and tetragonal forms is presented here. Both crystal forms were obtained by the vapor-diffusion technique and data were collected at 2.26 A (cubic crystal) and 2.60 A (tetragonal crystal) resolution. Two main differences were observed between these crystal structures: (i) whereas intermolecular contacts only involve salt-bridge type interactions via cadmium ions in the cubic structure, two types of interactions are observed in the tetragonal crystal (cadmium-ion-mediated salt bridges and hydrogen-bonding interactions) and (ii) cadmium ions bound in the threefold axes of ferritin molecules exhibit lower site-occupation factors in the tetragonal structure than in the cubic one.

About this Structure

1IER is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.

Reference

Comparison of the structures of the cubic and tetragonal forms of horse-spleen apoferritin., Granier T, Gallois B, Dautant A, Langlois d'Estaintot B, Precigoux G, Acta Crystallogr D Biol Crystallogr. 1997 Sep 1;53(Pt 5):580-7. PMID:15299889

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