3fi6: Difference between revisions
No edit summary |
No edit summary |
||
| (10 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
< | ==apo-H49AFr with high content of Pd ions== | ||
<StructureSection load='3fi6' size='340' side='right'caption='[[3fi6]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3fi6]] 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=3FI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FI6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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=PD:PALLADIUM+ION'>PD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3fi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fi6 OCA], [https://pdbe.org/3fi6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fi6 RCSB], [https://www.ebi.ac.uk/pdbsum/3fi6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fi6 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). | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fi/3fi6_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fi6 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Accumulation of metal ions on protein surfaces is an important subject in the field of materials science because these processes are applicable to the preparation of bioinspired inorganic materials. While previous studies related to this subject have focused on the preparation of nanomaterials using protein scaffolds, the detailed processes of metal ion deposition and metal core formation on a protein surface require clarification. Elucidation of the coordination structures of multinuclear metal binding sites on proteins at an early stage as well as intermediate and fully occupied stages of the metal ion deposition will help us to understand the reaction mechanisms so that desirable inorganic materials can be prepared using protein scaffolds. In this Article, we report on the detailed processes of accumulation of Pd(II) ions demonstrated by a series of X-ray crystal structural analyses of apo-ferritin (apo-Fr), an iron storage protein, containing different amounts of Pd(II) ions in the protein cage. We have identified the specific binding sites of Pd(II) ions and analyzed the dynamic changes in the coordination structure by a combination of the crystal structures and ICP quantitative analyses of apo-Fr containing low, intermediate, and high content of Pd(II) ions. Our studies on Pd(II).apo-Frs provide intriguing implications for the preparation of many other inorganic materials using protein surfaces. | |||
Process of Accumulation of Metal Ions on the Interior Surface of apo-Ferritin: Crystal Structures of a Series of apo-Ferritins Containing Variable Quantities of Pd(II) Ions.,Ueno T, Abe M, Hirata K, Abe S, Suzuki M, Shimizu N, Yamamoto M, Takata M, Watanabe Y J Am Chem Soc. 2009 Mar 24. PMID:19317403<ref>PMID:19317403</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3fi6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ferritin 3D structures|Ferritin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
< | |||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Abe | [[Category: Large Structures]] | ||
[[Category: Abe | [[Category: Abe M]] | ||
[[Category: Hirata | [[Category: Abe S]] | ||
[[Category: Shimizu | [[Category: Hirata K]] | ||
[[Category: Suzuki | [[Category: Shimizu N]] | ||
[[Category: Takata | [[Category: Suzuki M]] | ||
[[Category: Ueno | [[Category: Takata M]] | ||
[[Category: Watanabe | [[Category: Ueno T]] | ||
[[Category: Yamaoto | [[Category: Watanabe Y]] | ||
[[Category: Yamaoto M]] | |||