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| | <StructureSection load='4zl5' size='340' side='right'caption='[[4zl5]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='4zl5' size='340' side='right'caption='[[4zl5]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zl5]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Nitzschia_pungens_f._multiseries Nitzschia pungens f. multiseries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZL5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZL5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zl5]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudo-nitzschia_multiseries Pseudo-nitzschia multiseries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZL5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</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=4zl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zl5 OCA], [https://pdbe.org/4zl5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zl5 RCSB], [https://www.ebi.ac.uk/pdbsum/4zl5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zl5 ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zkh|4zkh]], [[4zkw|4zkw]], [[4zkx|4zkx]], [[4zl6|4zl6]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FTN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37319 Nitzschia pungens f. multiseries])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zl5 OCA], [http://pdbe.org/4zl5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zl5 RCSB], [http://www.ebi.ac.uk/pdbsum/4zl5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zl5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B6DMH6_PSEMU B6DMH6_PSEMU] 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.[RuleBase:RU361145] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ferritin|Ferritin]] | + | *[[Ferritin 3D structures|Ferritin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ferroxidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nitzschia pungens f. multiseries]] | + | [[Category: Pseudo-nitzschia multiseries]] |
| - | [[Category: Murphy, M E.P]] | + | [[Category: Murphy MEP]] |
| - | [[Category: Pfaffen, S]] | + | [[Category: Pfaffen S]] |
| - | [[Category: 4-helix bundle]]
| + | |
| - | [[Category: Di-iron ferroxidase centre]]
| + | |
| - | [[Category: Ferritin]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
B6DMH6_PSEMU 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.[RuleBase:RU361145]
Publication Abstract from PubMed
Ferritin from the marine pennate diatom Pseudo-nitzschia multiseries (PmFTN) plays a key role in sustaining growth in iron-limited ocean environments. The di-iron catalytic ferroxidase center of PmFTN (sites A and B) has a nearby third iron site (site C) in an arrangement typically observed in prokaryotic ferritins. Here we demonstrate that Glu44, a site C ligand, and Glu130, a residue that bridges iron bound at sites B and C, limit the rate of post-oxidation reorganization of iron coordination and the rate at which Fe3+ exits the ferroxidase center for storage within the mineral core. The latter, in particular, severely limits the overall rate of iron mineralization. Thus, the diatom ferritin is optimized for initial Fe2+ oxidation but not for mineralization, pointing to a role for this protein in buffering iron availability and facilitating iron-sparing rather than only long-term iron storage.
A Diatom Ferritin Optimized for Iron Oxidation but not Iron Storage.,Pfaffen S, Bradley JM, Abdulqadir R, Firme MR, Moore GR, Le Brun NE, Murphy ME J Biol Chem. 2015 Sep 22. pii: jbc.M115.669713. PMID:26396187[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pfaffen S, Bradley JM, Abdulqadir R, Firme MR, Moore GR, Le Brun NE, Murphy ME. A Diatom Ferritin Optimized for Iron Oxidation but not Iron Storage. J Biol Chem. 2015 Sep 22. pii: jbc.M115.669713. PMID:26396187 doi:http://dx.doi.org/10.1074/jbc.M115.669713
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