1OQU

A protein coordinated tri-nuclear Fe complex formed during soaking of crystals of the ribonucleotide reductase R2F protein from Corynebacterium Ammoniagenes

1OQU の概要

• エントリーDOI: 10.2210/pdb1oqu/pdb
• 関連するPDBエントリー: 1kgn 1kgo 1kgp
• 分子名称: ribonucleotide reductase subunit R2F, FE (III) ION, OXYGEN MOLECULE, ... (5 entities in total)
• 機能のキーワード: mineralization, ferritin, tri-iron, glutamate, metal binding protein
• 由来する生物種: Corynebacterium ammoniagenes
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 153108.03

構造登録者

Hogbom, M.,Nordlund, P. (登録日: 2003-03-11, 公開日: 2004-04-20, 最終更新日: 2024-03-13)

主引用文献

Hogbom, M.,Nordlund, P.
A protein carboxylate coordinated oxo-centered tri-nuclear iron complex with possible implications for ferritin mineralization
Febs Lett., 567:179-182, 2004

PubMed Abstract: The crystal structure of an oxo-centered tri-nuclear iron complex formed on a protein surface is presented. The cluster forms when crystals of the class Ib ribonucleotide reductase R2 protein from Corynebacterium ammoniagenes are subjected to iron soaking. The tri-iron-oxo complex is coordinated by protein-derived carboxylate ligands arranged in a motif similar to the one found on the inner surface of ferritins and may mimic an early stage in the mineralization of iron in ferritins. In addition, the structure adds to the very limited data on protein-mineral interfaces.

PubMed: 15178319
DOI: 10.1016/j.febslet.2004.04.068

実験手法

X-RAY DIFFRACTION (2 Å)