9qqh: Difference between revisions
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==Mini-bacterioferritin from Candidatus Methanoperedens species BLZ2 oxidized then chemically reduced== | |||
<StructureSection load='9qqh' size='340' side='right'caption='[[9qqh]], [[Resolution|resolution]] 2.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9qqh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidatus_Methanoperedens_sp._BLZ2 Candidatus Methanoperedens sp. BLZ2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9QQH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9QQH FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.08Å</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=FEC:1,3,5,8-TETRAMETHYL-PORPHINE-2,4,6,7-TETRAPROPIONIC+ACID+FERROUS+COMPLEX'>FEC</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=9qqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9qqh OCA], [https://pdbe.org/9qqh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9qqh RCSB], [https://www.ebi.ac.uk/pdbsum/9qqh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9qqh ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ferritins are ubiquitous among life forms, as they are essential for iron homeostasis. Here, we unveiled a novel member of the ferritin family, baptised mini-bacterioferritin. The characterised mini-bacterioferritin was isolated from a microbial enrichment dominated by the methanotrophic archaeon 'Candidatus Methanoperedens carboxydivorans'. Its atomic resolution crystal structure reveals a 12-mer assembly with a diiron ferroxidase centre located within a four-helix bundle. Redox-cycling experiments on protein crystals reveal a shift in iron position at the active site, which follows the established ferritin catalytic cycle. The 12-mer sphere-like structure harboured six Fe-coproporphyrin III ligands, positioned at the interdimeric interface, a characteristic previously only found in 24-mer bacterioferritins. Phylogenetics, together with structure predictions of closely related proteins, revealed that mini-bacterioferritins form a distinct clade within the ferritin family that might conserve ancestral traits. Future research will need to investigate the physiological roles of these enzymes, which were unsuspectingly widely distributed among prokaryotes. | |||
Mini-bacterioferritins: structural insight into a ferritin-like protein from the anaerobic methane-oxidising archaeon Candidatus Methanoperedens carboxydivorans.,Wissink M, Engilberge S, Leao P, Jansen RS, Jetten MSM, Belhamri M, Lemaire ON, Royant A, Welte CU, Wagner T Commun Biol. 2026 Mar 21. doi: 10.1038/s42003-026-09796-4. PMID:41865068<ref>PMID:41865068</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9qqh" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Candidatus Methanoperedens sp. BLZ2]] | |||
[[Category: Large Structures]] | |||
[[Category: Wagner T]] | |||
[[Category: Wissink M]] | |||
