2zg7: Difference between revisions

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==Crystal Structure of Pd(allyl)/apo-Fr==
==Crystal Structure of Pd(allyl)/apo-Fr==
<StructureSection load='2zg7' size='340' side='right' caption='[[2zg7]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='2zg7' size='340' side='right'caption='[[2zg7]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2zg7]] is a 1 chain structure with 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=2ZG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZG7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2zg7]] is a 1 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=2ZG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZG7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PLL:PALLADIUM(II)+ALLYL+COMPLEX'>PLL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.7&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zg8|2zg8]], [[2zg9|2zg9]]</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>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PLL:PALLADIUM(II)+ALLYL+COMPLEX'>PLL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</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=2zg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zg7 OCA], [https://pdbe.org/2zg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zg7 RCSB], [https://www.ebi.ac.uk/pdbsum/2zg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zg7 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zg7 OCA], [http://pdbe.org/2zg7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zg7 RCSB], [http://www.ebi.ac.uk/pdbsum/2zg7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zg7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Ferritin|Ferritin]]
*[[Ferritin 3D structures|Ferritin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Abe, M]]
[[Category: Large Structures]]
[[Category: Abe, S]]
[[Category: Abe M]]
[[Category: Erker, G]]
[[Category: Abe S]]
[[Category: Hikage, T]]
[[Category: Erker G]]
[[Category: Niemeyer, J]]
[[Category: Hikage T]]
[[Category: Ueno, T]]
[[Category: Niemeyer J]]
[[Category: Watanabe, Y]]
[[Category: Ueno T]]
[[Category: Artificial metalloprotein]]
[[Category: Watanabe Y]]
[[Category: Iron storage protein]]
[[Category: Light chain apoferritin]]
[[Category: Metal binding protein]]

Latest revision as of 16:35, 1 November 2023

Crystal Structure of Pd(allyl)/apo-FrCrystal Structure of Pd(allyl)/apo-Fr

Structural highlights

2zg7 is a 1 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 1.7Å
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

We report the preparation of organometallic Pd(allyl) dinuclear complexes in protein cages of apo-Fr by reactions with [Pd(allyl)Cl]2 (allyl = eta3-C3H5). One of the dinuclear complexes is converted to a trinuclear complex by replacing a Pd-coordinated His residue to an Ala residue. These results suggest that multinuclear metal complexes with various coordination structures could be prepared by the deletion or introduction of His, Cys, and Glu at appropriate positions on protein surface.

Control of the coordination structure of organometallic palladium complexes in an apo-ferritin cage.,Abe S, Niemeyer J, Abe M, Takezawa Y, Ueno T, Hikage T, Erker G, Watanabe Y J Am Chem Soc. 2008 Aug 13;130(32):10512-4. Epub 2008 Jul 18. PMID:18636721[1]

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

See Also

References

  1. Abe S, Niemeyer J, Abe M, Takezawa Y, Ueno T, Hikage T, Erker G, Watanabe Y. Control of the coordination structure of organometallic palladium complexes in an apo-ferritin cage. J Am Chem Soc. 2008 Aug 13;130(32):10512-4. Epub 2008 Jul 18. PMID:18636721 doi:10.1021/ja802463a

2zg7, resolution 1.70Å

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