1SQ3

Crystal structures of a novel open pore ferritin from the hyperthermophilic Archaeon Archaeoglobus fulgidus.

1SQ3 の概要

• エントリーDOI: 10.2210/pdb1sq3/pdb
• 関連するPDBエントリー: 1S3Q
• 分子名称: ferritin, FE (III) ION (3 entities in total)
• 機能のキーワード: ferroxidase, four helix bundle, iron storage, metal binding protein
• 由来する生物種: Archaeoglobus fulgidus
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 251132.09

構造登録者

Johnson, E.,Cascio, D.,Michael, S.,Schroder, I. (登録日: 2004-03-17, 公開日: 2005-04-12, 最終更新日: 2024-10-30)

主引用文献

Johnson, E.,Cascio, D.,Sawaya, M.R.,Gingery, M.,Schroder, I.
Crystal structures of a tetrahedral open pore ferritin from the hyperthermophilic archaeon Archaeoglobus fulgidus.
Structure, 13:637-648, 2005

PubMed Abstract: Ferritins are known as important iron storage/detoxification proteins and are widely found in living organisms. This report details the 2.1 A resolution native and 2.7 A resolution iron bound structures of the ferritin from the hyperthermophilic Archaeon Archaeoglobus fulgidus, and represents the first structure of a ferritin from an archaeon, or a hyperthermophilic organism. The A. fulgidus ferritin (AfFtn) monomer has a high degree of structural similarity with archetypal ferritins from E. coli and humans, but the AfFtn quaternary structure is novel; 24 subunits assemble into a shell having tetrahedral (2-3) rather than the canonical octahedral (4-3-2) symmetry of archetypal ferritins. The difference in assembly opens four large (approximately 45 A) pores in the AfFtn shell. Two nonconservative amino acid substitutions may be critical for stabilizing the tetrahedral form.

PubMed: 15837202
DOI: 10.1016/j.str.2005.01.019

実験手法

X-RAY DIFFRACTION (2.7 Å)