5obb: Difference between revisions
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==Structure of a modified mouse H chain ferritin with a lanthanide binding motif in complex with Terbium== | ==Structure of a modified mouse H chain ferritin with a lanthanide binding motif in complex with Terbium== | ||
<StructureSection load='5obb' size='340' side='right' caption='[[5obb]], [[Resolution|resolution]] 2.65Å' scene=''> | <StructureSection load='5obb' size='340' side='right'caption='[[5obb]], [[Resolution|resolution]] 2.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5obb]] is a 24 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5obb]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OBB FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TB:TERBIUM(III)+ION'>TB</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5obb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5obb OCA], [https://pdbe.org/5obb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5obb RCSB], [https://www.ebi.ac.uk/pdbsum/5obb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5obb ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/FRIH_MOUSE FRIH_MOUSE] Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. 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.<ref>PMID:19154717</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5obb" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5obb" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ferritin 3D structures|Ferritin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Baiocco | [[Category: Baiocco P]] | ||
[[Category: Trabuco | [[Category: Trabuco MC]] | ||
Latest revision as of 12:39, 6 December 2023
Structure of a modified mouse H chain ferritin with a lanthanide binding motif in complex with TerbiumStructure of a modified mouse H chain ferritin with a lanthanide binding motif in complex with Terbium
Structural highlights
FunctionFRIH_MOUSE Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. 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.[1] Publication Abstract from PubMedFerritin H-homopolymers have been extensively used as nanocarriers for diverse applications in the targeted delivery of drugs and imaging agents, due to their unique ability to bind the transferrin receptor (CD71), highly overexpressed in most tumor cells. In order to incorporate novel fluorescence imaging properties, we have fused a lanthanide binding tag (LBT) to the C-terminal end of mouse H-chain ferritin, HFt. The HFt-LBT possesses one high affinity Terbium binding site per each of the 24 subunits provided by six coordinating aminoacid side chains and a tryptophan residue in its close proximity and is thus endowed with strong FRET sensitization properties. Accordingly, the characteristic Terbium emission band at 544 nm for the HFt-LBT Tb(III) complex was detectable upon excitation of the tag enclosed at two order of magnitude higher intensity with respect to the wtHFt protein. X-ray data at 2.9 A and cryo-EM at 7 A resolution demonstrated that HFt-LBT is correctly assembled as a 24-mer both in crystal and in solution. On the basis of the intrinsic Tb(III) binding properties of the wt protein, 32 additional Tb(III) binding sites, located within the natural iron binding sites of the protein, were identified besides the 24 Tb(III) ions coordinated to the LBTs. HFt-LBT Tb(III) was demonstrated to be actively uptaken by selected tumor cell lines by confocal microscopy and FACS analysis of their FITC derivatives, although direct fluorescence from Terbium emission could not be singled out with conventional, 295-375 nm, fluorescence excitation. Engineered ferritin for lanthanide binding.,Calisti L, Trabuco MC, Boffi A, Testi C, Montemiglio LC, des Georges A, Benni I, Ilari A, Taciak B, Bialasek M, Rygiel T, Krol M, Baiocco P, Bonamore A PLoS One. 2018 Aug 13;13(8):e0201859. doi: 10.1371/journal.pone.0201859., eCollection 2018. PMID:30102720[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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