2JD8

Crystal Structure of the Zn-soaked Ferritin from the Hyperthermophilic Archaeal Anaerobe Pyrococcus furiosus

2JD8 の概要

• エントリーDOI: 10.2210/pdb2jd8/pdb
• 関連するPDBエントリー: 2JD6 2JD7
• 分子名称: FERRITIN HOMOLOG, ZINC ION, FE (III) ION, ... (5 entities in total)
• 機能のキーワード: metal transport, ferritin, iron, archaeon, hyperthermophile, ferroxidase center, thermostability, entry channels, pores metal transport
• 由来する生物種: PYROCOCCUS FURIOSUS
• タンパク質・核酸の鎖数: 36
• 化学式量合計: 742939.07

構造登録者

Tatur, J.,Hagen, W.R.,Matias, P.M. (登録日: 2007-01-05, 公開日: 2007-02-27, 最終更新日: 2023-12-13)

主引用文献

Tatur, J.,Hagen, W.R.,Matias, P.M.
Crystal Structure of the Ferritin from the Hyperthermophilic Archaeal Anaerobe Pyrococcus Furiosus
J.Biol.Inorg.Chem., 12:615-, 2007

PubMed Abstract: The crystal structure of the ferritin from the archaeon, hyperthermophile and anaerobe Pyrococcus furiosus (PfFtn) is presented. While many ferritin structures from bacteria to mammals have been reported, until now only one was available from archaea, the ferritin from Archaeoglobus fulgidus (AfFtn). The PfFtn 24-mer exhibits the 432 point-group symmetry that is characteristic of most ferritins, which suggests that the 23 symmetry found in the previously reported AfFtn is not a common feature of archaeal ferritins. Consequently, the four large pores that were found in AfFtn are not present in PfFtn. The structure has been solved by molecular replacement and refined at 2.75-Angstrom resolution to R = 0.195 and R(free) = 0.247. The ferroxidase center of the aerobically crystallized ferritin contains one iron at site A and shows sites B and C only upon iron or zinc soaking. Electron paramagnetic resonance studies suggest this iron depletion of the native ferroxidase center to be a result of a complexation of iron by the crystallization salt. The extreme thermostability of PfFtn is compared with that of eight structurally similar ferritins and is proposed to originate mostly from the observed high number of intrasubunit hydrogen bonds. A preservation of the monomer fold, rather than the 24-mer assembly, appears to be the most important factor that protects the ferritin from inactivation by heat.

PubMed: 17541801
DOI: 10.1007/S00775-007-0212-3

実験手法

X-RAY DIFFRACTION (2.8 Å)