3GVY

Crystal structure of bacterioferritin from R.sphaeroides

3GVY の概要

• エントリーDOI: 10.2210/pdb3gvy/pdb
• 分子名称: Bacterioferritin, PROTOPORPHYRIN IX CONTAINING FE, FE (III) ION (3 entities in total)
• 機能のキーワード: bacterioferritin, ferritin, iron storage, di-iron, ferroxidase activity, heme, metal binding protein
• 由来する生物種: Rhodobacter sphaeroides
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 57082.95

構造登録者

Hwang, K.Y.,Nam, K.H. (登録日: 2009-03-31, 公開日: 2009-12-22, 最終更新日: 2023-11-01)

主引用文献

Nam, K.H.,Xu, Y.,Piao, S.,Priyadarshi, A.,Lee, E.H.,Kim, H.-Y.,Jeon, Y.H.,Ha, N.-C.,Hwang, K.Y.
Crystal structure of bacterioferritin from Rhodobacter sphaeroides
Biochem.Biophys.Res.Commun., 391:990-994, 2010

PubMed Abstract: Iron is essential for the survival of organisms, but either excess or deficient levels of iron induce oxidative stress, thereby causing cell damage. As a result, iron regulation is essential for proper cell growth and proliferation in most organisms. Bacterioferritin is a ferritin-like family protein that contains a heme molecule and a ferroxidase site at the di-iron center. This protein plays a primary role in intracellular iron storage for iron homeostasis, as well as in the maintenance of iron in a soluble and non-toxic form. Although several bacterioferritin structures have been determined, no structural studies have successfully elucidated the molecular function of the heme molecule and the ferroxidase center. Here, we report the crystal structure of bacterioferritin from Rhodobacter sphaeroides. This protein exists in a roughly spherical configuration via the assembly of 24 subunits. We describe the oligomeric arrangement, ferroxidase center and heme-binding site based on this structure. The protein contains a single iron-binding configuration in the ferroxidase center, which allows for the release of iron by His130 when the protein is in the intermediate state. The heme molecule in RsBfr is stabilized by shifting of the van der Waals interaction center between the porphyrin of the heme and Trp26. We anticipate that further structural analysis will provide a more complete understanding of the molecular mechanisms of members of the ferritin-like family.

PubMed: 19968959
DOI: 10.1016/j.bbrc.2009.12.003

実験手法

X-RAY DIFFRACTION (2.8 Å)