7viq: Difference between revisions
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==Crystal structure of Au(50EQ)-apo-R168H/L169C-rHLFr== | ==Crystal structure of Au(50EQ)-apo-R168H/L169C-rHLFr== | ||
<StructureSection load='7viq' size='340' side='right'caption='[[7viq]]' scene=''> | <StructureSection load='7viq' size='340' side='right'caption='[[7viq]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VIQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[7viq]] 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=7VIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VIQ FirstGlance]. <br> | ||
</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=7viq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7viq OCA], [https://pdbe.org/7viq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7viq RCSB], [https://www.ebi.ac.uk/pdbsum/7viq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7viq ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</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=7viq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7viq OCA], [https://pdbe.org/7viq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7viq RCSB], [https://www.ebi.ac.uk/pdbsum/7viq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7viq ProSAT]</span></td></tr> | |||
</table> | </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 == | |||
Water-soluble and biocompatible protein-protected gold nanoclusters (Au NCs) hold great promise for numerous applications. However, design and precise regulation of their structure at an atomic level remain challenging. Herein, we have engineered and constructed a gold clustering site at the 4-fold symmetric axis channel of the apo-ferritin cage. Using a series of X-ray crystal structures, we evaluated the stepwise accumulation process of Au ions into the cage and the formation of a multinuclear Au cluster in our designed cavity. We also disclosed the role of key residues in the metal accumulation process. X-ray crystal structures in combination with quantum chemical (QC) calculation revealed a unique Au clustering site with up to 12 Au atoms positions in the cavity. Moreover, the structure of the gold nanocluster was precisely tuned by the dosage of the Au precursor. As the gold concentration increases, the number of Au atoms position at the clustering site increases from 8 to 12, and a structural rearrangement was observed at a higher Au concentration. Furthermore, the binding affinity order of the four Au binding sites on apo-ferritin was unveiled with a stepwise increase of Au precursor concentration. | |||
Design of a gold clustering site in an engineered apo-ferritin cage.,Lu C, Maity B, Peng X, Ito N, Abe S, Sheng X, Ueno T, Lu D Commun Chem. 2022 Mar 21;5(1):39. doi: 10.1038/s42004-022-00651-1. PMID:36697940<ref>PMID:36697940</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7viq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Equus caballus]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Abe S]] | [[Category: Abe S]] | ||
Revision as of 09:58, 8 February 2023
Crystal structure of Au(50EQ)-apo-R168H/L169C-rHLFrCrystal structure of Au(50EQ)-apo-R168H/L169C-rHLFr
Structural highlights
FunctionFRIL_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). Publication Abstract from PubMedWater-soluble and biocompatible protein-protected gold nanoclusters (Au NCs) hold great promise for numerous applications. However, design and precise regulation of their structure at an atomic level remain challenging. Herein, we have engineered and constructed a gold clustering site at the 4-fold symmetric axis channel of the apo-ferritin cage. Using a series of X-ray crystal structures, we evaluated the stepwise accumulation process of Au ions into the cage and the formation of a multinuclear Au cluster in our designed cavity. We also disclosed the role of key residues in the metal accumulation process. X-ray crystal structures in combination with quantum chemical (QC) calculation revealed a unique Au clustering site with up to 12 Au atoms positions in the cavity. Moreover, the structure of the gold nanocluster was precisely tuned by the dosage of the Au precursor. As the gold concentration increases, the number of Au atoms position at the clustering site increases from 8 to 12, and a structural rearrangement was observed at a higher Au concentration. Furthermore, the binding affinity order of the four Au binding sites on apo-ferritin was unveiled with a stepwise increase of Au precursor concentration. Design of a gold clustering site in an engineered apo-ferritin cage.,Lu C, Maity B, Peng X, Ito N, Abe S, Sheng X, Ueno T, Lu D Commun Chem. 2022 Mar 21;5(1):39. doi: 10.1038/s42004-022-00651-1. PMID:36697940[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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