4XKU

E coli BFR variant Y114F

4XKU の概要

• エントリーDOI: 10.2210/pdb4xku/pdb
• 分子名称: Bacterioferritin, SULFATE ION (3 entities in total)
• 機能のキーワード: iron storage, diiron site, metal binding protein
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 223465.14

構造登録者

Hemmings, A.M.,Le Brun, N.E.,Bradley, J.M. (登録日: 2015-01-12, 公開日: 2015-12-16, 最終更新日: 2024-01-10)

主引用文献

Bradley, J.M.,Svistunenko, D.A.,Lawson, T.L.,Hemmings, A.M.,Moore, G.R.,Le Brun, N.E.
Three Aromatic Residues are Required for Electron Transfer during Iron Mineralization in Bacterioferritin.
Angew.Chem.Int.Ed.Engl., 54:14763-14767, 2015

PubMed Abstract: Ferritins are iron storage proteins that overcome the problems of toxicity and poor bioavailability of iron by catalyzing iron oxidation and mineralization through the activity of a diiron ferroxidase site. Unlike in other ferritins, the oxidized di-Fe(3+) site of Escherichia coli bacterioferritin (EcBFR) is stable and therefore does not function as a conduit for the transfer of Fe(3+) into the storage cavity, but instead acts as a true catalytic cofactor that cycles its oxidation state while driving Fe(2+) oxidation in the cavity. Herein, we demonstrate that EcBFR mineralization depends on three aromatic residues near the diiron site, Tyr25, Tyr58, and Trp133, and that a transient radical is formed on Tyr25. The data indicate that the aromatic residues, together with a previously identified inner surface iron site, promote mineralization by ensuring the simultaneous delivery of two electrons, derived from Fe(2+) oxidation in the BFR cavity, to the di-ferric catalytic site for safe reduction of O2.

PubMed: 26474305
DOI: 10.1002/anie.201507486

実験手法

X-RAY DIFFRACTION (1.78 Å)