6lpe: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6lpe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Phascolosoma_esculenta Phascolosoma esculenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LPE FirstGlance]. <br>
<table><tr><td colspan='2'>[[6lpe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Phascolosoma_esculenta Phascolosoma esculenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LPE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.99&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ferroxidase Ferroxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6lpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lpe OCA], [https://pdbe.org/6lpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lpe RCSB], [https://www.ebi.ac.uk/pdbsum/6lpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lpe ProSAT]</span></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=6lpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lpe OCA], [https://pdbe.org/6lpe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lpe RCSB], [https://www.ebi.ac.uk/pdbsum/6lpe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lpe ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/B3TFG2_9BILA B3TFG2_9BILA]] 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.[ARBA:ARBA00002716]  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]  
[https://www.uniprot.org/uniprot/B3TFG2_9BILA B3TFG2_9BILA] 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.[ARBA:ARBA00002716]  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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</div>
</div>
<div class="pdbe-citations 6lpe" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6lpe" style="background-color:#fffaf0;"></div>
==See Also==
*[[Ferritin 3D structures|Ferritin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ferroxidase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Phascolosoma esculenta]]
[[Category: Phascolosoma esculenta]]
[[Category: Ming, T H]]
[[Category: Ming TH]]
[[Category: Su, X R]]
[[Category: Su XR]]
[[Category: Crystal structure]]
[[Category: Ferritin]]
[[Category: Oxidoreductase]]
[[Category: Ribosomal protein]]

Latest revision as of 17:42, 29 November 2023

Phascolosoma esculenta ferritinPhascolosoma esculenta ferritin

Structural highlights

6lpe is a 4 chain structure with sequence from Phascolosoma esculenta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.99Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B3TFG2_9BILA 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.[ARBA:ARBA00002716] 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

For marine invertebrates with no adaptive immune system, ferritin is a major intracellular iron-storage protein with a critical role in innate immunity. Here, we present the crystal structures of two novel ferritins (Fer147 and PeFer) from the marine invertebrate Phascolosoma esculenta, which resides in muddy-bottom coastal regions. Fer147 and PeFer exhibit the 4-3-2 symmetry of cage-like hollow shells containing 24 subunits, similar to other known ferritins. Fer147 and PeFer contain both the conserved ferroxidase center and 3-fold channels. Subtle structural differences in the putative nucleation sites suggest possible routes of metal ion movement in the protein shells. However, the marked variation in the electrostatic potential of the 3-fold channels in Fer147 and the 4-fold channels in PeFer suggest significant diversity between Fer147 and PeFer in terms of metal ion aggregation and cation exclusion. In summary, the presented crystal structures may serve as references for studies of the iron storage mechanism of additional ferritins from marine invertebrates.

Structural comparison of two ferritins from the marine invertebrate Phascolosoma esculenta.,Ming T, Huan H, Su C, Huo C, Wu Y, Jiang Q, Qiu X, Lu C, Zhou J, Li Y, Su X FEBS Open Bio. 2021 Jan 15. doi: 10.1002/2211-5463.13080. PMID:33448656[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Ming T, Huan H, Su C, Huo C, Wu Y, Jiang Q, Qiu X, Lu C, Zhou J, Li Y, Su X. Structural comparison of two ferritins from the marine invertebrate Phascolosoma esculenta. FEBS Open Bio. 2021 Jan 15. doi: 10.1002/2211-5463.13080. PMID:33448656 doi:http://dx.doi.org/10.1002/2211-5463.13080

6lpe, resolution 1.99Å

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OCA