3a68: Difference between revisions
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<StructureSection load='3a68' size='340' side='right'caption='[[3a68]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='3a68' size='340' side='right'caption='[[3a68]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3a68]] is a 24 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3a68]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A68 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]] 1.8Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=3a68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a68 OCA], [https://pdbe.org/3a68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a68 RCSB], [https://www.ebi.ac.uk/pdbsum/3a68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a68 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/FRI4_SOYBN FRI4_SOYBN] 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 (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Glycine max]] | |||
[[Category: Glycine | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Goto | [[Category: Goto F]] | ||
[[Category: Masuda | [[Category: Masuda T]] | ||
[[Category: Mikami | [[Category: Mikami B]] | ||
[[Category: Yoshihara | [[Category: Yoshihara T]] | ||
Latest revision as of 17:13, 1 November 2023
Crystal structure of plant ferritin reveals a novel metal binding site that functions as a transit site for metal transfer in ferritinCrystal structure of plant ferritin reveals a novel metal binding site that functions as a transit site for metal transfer in ferritin
Structural highlights
FunctionFRI4_SOYBN 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 (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFerritins are important iron storage and detoxification proteins that are widely distributed in living kingdoms. Because plant ferritin possesses both a ferroxidase site and a ferrihydrite nucleation site, it is a suitable model for studying the mechanism of iron storage in ferritin. This article presents for the first time the crystal structure of a plant ferritin from soybean at 1.8-A resolution. The soybean ferritin 4 (SFER4) had a high structural similarity to vertebrate ferritin, except for the N-terminal extension region, the C-terminal short helix E, and the end of the BC-loop. Similar to the crystal structures of other ferritins, metal binding sites were observed in the iron entry channel, ferroxidase center, and nucleation site of SFER4. In addition to these conventional sites, a novel metal binding site was discovered intermediate between the iron entry channel and the ferroxidase site. This site was coordinated by the acidic side chain of Glu(173) and carbonyl oxygen of Thr(168), which correspond, respectively, to Glu(140) and Thr(135) of human H chain ferritin according to their sequences. A comparison of the ferroxidase activities of the native and the E173A mutant of SFER4 clearly showed a delay in the iron oxidation rate of the mutant. This indicated that the glutamate residue functions as a transit site of iron from the 3-fold entry channel to the ferroxidase site, which may be universal among ferritins. Crystal structure of plant ferritin reveals a novel metal binding site that functions as a transit site for metal transfer in ferritin.,Masuda T, Goto F, Yoshihara T, Mikami B J Biol Chem. 2010 Feb 5;285(6):4049-59. Epub 2009 Dec 9. PMID:20007325[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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