9QQH

Mini-bacterioferritin from Candidatus Methanoperedens species BLZ2 oxidized then chemically reduced

9QQH の概要

• エントリーDOI: 10.2210/pdb9qqh/pdb
• 分子名称: Bacterioferritin, FE (III) ION, 1,3,5,8-TETRAMETHYL-PORPHINE-2,4,6,7-TETRAPROPIONIC ACID FERROUS COMPLEX, ... (4 entities in total)
• 機能のキーワード: ferritin-like protein, mini-ferritin, fe-coproporphyrin iii, anaerobic methane-oxidising archaea, archaea, iron homeostasis, iron storage, dodecamer, nano-compartment, chemical reduction, oxidoreductase
• 由来する生物種: Candidatus Methanoperedens sp. BLZ2
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 65796.13

構造登録者

Wissink, M.,Wagner, T. (登録日: 2025-03-31, 公開日: 2026-04-01)

主引用文献

Wissink, M.,Engilberge, S.,Leao, P.,Jansen, R.S.,Jetten, M.S.M.,Belhamri, M.,Lemaire, O.N.,Royant, A.,Welte, C.U.,Wagner, T.
Mini-bacterioferritins: structural insight into a ferritin-like protein from the anaerobic methane-oxidising archaeon Candidatus Methanoperedens carboxydivorans.
Commun Biol, 2026

PubMed Abstract: 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.

PubMed: 41865068
DOI: 10.1038/s42003-026-09796-4

実験手法

X-RAY DIFFRACTION (2.08 Å)