3af9: Difference between revisions

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-[[Image:3af9.png|left|200px]]
-{{STRUCTURE_3af9|  PDB=3af9  |  SCENE=  }}
+==Crystal Structure of Pd(allyl)/apo-C48AFr==
+<StructureSection load='3af9' size='340' side='right'caption='[[3af9]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3af9]] 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=3AF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AF9 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]] 1.85&#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>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PD:PALLADIUM+ION'>PD</scene>, <scene name='pdbligand=PLL:PALLADIUM(II)+ALLYL+COMPLEX'>PLL</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=3af9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3af9 OCA], [https://pdbe.org/3af9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3af9 RCSB], [https://www.ebi.ac.uk/pdbsum/3af9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3af9 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/af/3af9_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=3af9 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Hybridization of metal complexes and protein scaffolds is an important subject in bioinorganic chemistry and materials science. Efforts to provide non-natural functions to proteins will likely lead to advances in development of catalysts, sensors, and so on. Mechanistic investigations of the process of binding of metal complexes within protein scaffolds and characterization of the resulting coordination structures will help us to design and control coordination structures of metal complexes for construction of hybrid proteins containing metal complexes. In this work, the processes of accumulation and incorporation of organometallic palladium complexes within the cage of the iron storage protein apo-ferritin (apo-Fr) are elucidated by analysis of X-ray crystal structures of apo-Fr and selected mutants thereof, in the presence of the metal complexes. The crystal structure of apo-Fr containing Pd(allyl) (allyl = eta(3)-C(3)H(5)) complexes shows that thiolato-bridged dinuclear Pd(allyl) complexes are formed at two binding sites within the cage of apo-Fr. The crystal structures of apo-Fr and its Cys- and His-deletion mutants containing Pd(allyl) complexes indicate that Cys126 accelerates the incorporation of Pd(allyl) complexes into the cage. In addition, Cys48 and Cys126 are essential for accumulation of Pd(allyl) complexes and stabilizing the square planar coordination structure.
-===Crystal Structure of Pd(allyl)/apo-C48AFr===
+Mechanism of accumulation and incorporation of organometallic Pd complexes into the protein nanocage of apo-ferritin.,Abe S, Hikage T, Watanabe Y, Kitagawa S, Ueno T Inorg Chem. 2010 Aug 2;49(15):6967-73. PMID:20586408<ref>PMID:20586408</ref>
-{{ABSTRACT_PUBMED_20586408}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 3af9" style="background-color:#fffaf0;"></div>
-[[3af9]] is a 1 chain structure of [[Ferritin]] 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=3AF9 OCA].
 ==See Also==
-*[[Ferritin|Ferritin]]
+*[[Ferritin 3D structures|Ferritin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:020586408</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Equus caballus]]
-[[Category: Abe, S.]]
+[[Category: Large Structures]]
-[[Category: Hikage, T.]]
+[[Category: Abe S]]
-[[Category: Kitagawa, S.]]
+[[Category: Hikage T]]
-[[Category: Ueno, T.]]
+[[Category: Kitagawa S]]
-[[Category: Watanabe, Y.]]
+[[Category: Ueno T]]
-[[Category: Artificial metalloprotein]]
+[[Category: Watanabe Y]]
-[[Category: Iron storage protein]]
-[[Category: Light chain ferritin]]
-[[Category: Metal binding protein]]