1ies

From Proteopedia

(Difference between revisions)

Current revision

TETRAGONAL CRYSTAL STRUCTURE OF NATIVE HORSE SPLEEN FERRITIN

Structural highlights

1ies is a 6 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FRIL_HORSE Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Granier T, Gallois B, Dautant A, Langlois d'Estaintot B, Precigoux G. Comparison of the structures of the cubic and tetragonal forms of horse-spleen apoferritin. Acta Crystallogr D Biol Crystallogr. 1997 Sep 1;53(Pt 5):580-7. PMID:15299889 doi:10.1107/S0907444997003314

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ies"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1ies]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IES FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ies FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ies OCA], [https://pdbe.org/1ies PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ies RCSB], [https://www.ebi.ac.uk/pdbsum/1ies PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ies ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/FRIL_HORSE FRIL_HORSE]] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).
+[https://www.uniprot.org/uniprot/FRIL_HORSE FRIL_HORSE] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 38: @@
 [[Category: Equus caballus]]
 [[Category: Large Structures]]
-[[Category: Dautant, A]]
+[[Category: Dautant A]]
-[[Category: Estaintot, B Langlois D]]
+[[Category: Gallois B]]
-[[Category: Gallois, B]]
+[[Category: Granier T]]
-[[Category: Granier, T]]
+[[Category: Langlois D'Estaintot B]]
-[[Category: Precigoux, G]]
+[[Category: Precigoux G]]
-[[Category: Apoferritin]]
-[[Category: Iron storage]]

1ies

From Proteopedia

Current revision

TETRAGONAL CRYSTAL STRUCTURE OF NATIVE HORSE SPLEEN FERRITIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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