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==Crystal structure of Haliangium ochraceum encapsulated ferritin== | ==Crystal structure of Haliangium ochraceum encapsulated ferritin== | ||
<StructureSection load='5n5f' size='340' side='right' caption='[[5n5f]], [[Resolution|resolution]] 2.06Å' scene=''> | <StructureSection load='5n5f' size='340' side='right'caption='[[5n5f]], [[Resolution|resolution]] 2.06Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5n5f]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N5F OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5n5f]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Haliangium_ochraceum Haliangium ochraceum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N5F FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.057Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=5n5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n5f OCA], [https://pdbe.org/5n5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n5f RCSB], [https://www.ebi.ac.uk/pdbsum/5n5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n5f ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/D0LZ73_HALO1 D0LZ73_HALO1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ferritins are a large family of intracellular proteins that protect the cell from oxidative stress by catalytically converting Fe(II) into less toxic Fe(III) and storing iron minerals within their core. Encapsulated ferritins (EncFtn) are a sub-family of ferritin-like proteins, which are widely distributed in all bacterial and archaeal phyla. The recently characterized Rhodospirillum rubrum EncFtn displays an unusual structure when compared with classical ferritins, with an open decameric structure that is enzymatically active, but unable to store iron. This EncFtn must be associated with an encapsulin nanocage in order to act as an iron store. Given the wide distribution of the EncFtn family in organisms with diverse environmental niches, a question arises as to whether this unusual structure is conserved across the family. Here, we characterize EncFtn proteins from the halophile Haliangium ochraceum and the thermophile Pyrococcus furiosus, which show the conserved annular pentamer of dimers topology. Key structural differences are apparent between the homologues, particularly in the centre of the ring and the secondary metal-binding site, which is not conserved across the homologues. Solution and native mass spectrometry analyses highlight that the stability of the protein quaternary structure differs between EncFtn proteins from different species. The ferroxidase activity of EncFtn proteins was confirmed, and we show that while the quaternary structure around the ferroxidase centre is distinct from classical ferritins, the ferroxidase activity is still inhibited by Zn(II). Our results highlight the common structural organization and activity of EncFtn proteins, despite diverse host environments and contexts within encapsulins. | |||
Conservation of the structural and functional architecture of encapsulated ferritins in bacteria and archaea.,He D, Piergentili C, Ross J, Tarrant E, Tuck LR, Mackay CL, McIver Z, Waldron KJ, Clarke DJ, Marles-Wright J Biochem J. 2019 Mar 22;476(6):975-989. doi: 10.1042/BCJ20180922. PMID:30837306<ref>PMID:30837306</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5n5f" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ferritin 3D structures|Ferritin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Haliangium ochraceum]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: He D]] | ||
[[Category: | [[Category: Marles-Wright J]] | ||
Latest revision as of 21:03, 8 November 2023
Crystal structure of Haliangium ochraceum encapsulated ferritinCrystal structure of Haliangium ochraceum encapsulated ferritin
Structural highlights
FunctionPublication Abstract from PubMedFerritins are a large family of intracellular proteins that protect the cell from oxidative stress by catalytically converting Fe(II) into less toxic Fe(III) and storing iron minerals within their core. Encapsulated ferritins (EncFtn) are a sub-family of ferritin-like proteins, which are widely distributed in all bacterial and archaeal phyla. The recently characterized Rhodospirillum rubrum EncFtn displays an unusual structure when compared with classical ferritins, with an open decameric structure that is enzymatically active, but unable to store iron. This EncFtn must be associated with an encapsulin nanocage in order to act as an iron store. Given the wide distribution of the EncFtn family in organisms with diverse environmental niches, a question arises as to whether this unusual structure is conserved across the family. Here, we characterize EncFtn proteins from the halophile Haliangium ochraceum and the thermophile Pyrococcus furiosus, which show the conserved annular pentamer of dimers topology. Key structural differences are apparent between the homologues, particularly in the centre of the ring and the secondary metal-binding site, which is not conserved across the homologues. Solution and native mass spectrometry analyses highlight that the stability of the protein quaternary structure differs between EncFtn proteins from different species. The ferroxidase activity of EncFtn proteins was confirmed, and we show that while the quaternary structure around the ferroxidase centre is distinct from classical ferritins, the ferroxidase activity is still inhibited by Zn(II). Our results highlight the common structural organization and activity of EncFtn proteins, despite diverse host environments and contexts within encapsulins. Conservation of the structural and functional architecture of encapsulated ferritins in bacteria and archaea.,He D, Piergentili C, Ross J, Tarrant E, Tuck LR, Mackay CL, McIver Z, Waldron KJ, Clarke DJ, Marles-Wright J Biochem J. 2019 Mar 22;476(6):975-989. doi: 10.1042/BCJ20180922. PMID:30837306[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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