View source for 9kpa


==Crystal structure of Horse spleen L-ferritin mutant (R59F)==
<StructureSection load='9kpa' size='340' side='right'caption='[[9kpa]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9kpa]] 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=9KPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9KPA 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]] 1.5&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=9kpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9kpa OCA], [https://pdbe.org/9kpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9kpa RCSB], [https://www.ebi.ac.uk/pdbsum/9kpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9kpa 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).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Dynamic behavior of proteins, such as orientation changes of aromatic residues, plays an important role in controlling biomolecular functions. Protein design that can precisely control such dynamic behavior at the atomic level is a challenging issue. The study reports the development of a system capable of orientational changes of aromatic side chains upon ligand binding. Aromatic pockets are constructed on the inner surfaces of protein cages to bind polycyclic aromatic fluorescent molecules to the targeted position by pi-pi stacking interactions. X-ray crystal structural analysis indicated the cooperative orientation changes of the aromatic clusters around the pocket triggered by the ligand binding. A comparison of various ligands shows that the movement of aromatic clusters can be controlled depending on the ligand structures. Fluorescence quantum yield and fluorescence lifetime are enhanced due to isolation of the fluorescent molecules in an aromatic pocket. These findings provide an understanding of the unique molecular behavior and fluorescence properties of ligands due to the assembly of aromatic residues and a guideline for developing dynamically controlled supramolecular biomaterials.

Design of Aromatic Interaction Networks in a Protein Cage Modulated by Fluorescent Ligand Binding.,Hishikawa Y, Suzuki T, Maity B, Noya H, Yoshizawa M, Asanuma A, Katagiri Y, Abe S, Nagatoishi S, Tsumoto K, Ueno T Adv Sci (Weinh). 2025 Feb 20:e2417030. doi: 10.1002/advs.202417030. PMID:39973762<ref>PMID:39973762</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9kpa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Equus caballus]]
[[Category: Large Structures]]
[[Category: Abe S]]
[[Category: Hishikawa Y]]
[[Category: Maity B]]
[[Category: Suzuki T]]
[[Category: Ueno T]]