3ES3

Directing Noble Metal Ion Chemistry within a Designed Ferritin Protein. The Complex with Gold ions. Ferritin H8-H9x Mutant

3ES3 の概要

• エントリーDOI: 10.2210/pdb3es3/pdb
• 関連するPDBエントリー: 2Z6M 3ERZ
• 分子名称: Ferritin heavy chain, GOLD ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: nanoparticle synthesis, gold ions, ferritin, mutant, iron, iron storage, metal-binding, oxidoreductase, phosphoprotein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21991.52

構造登録者

Di Costanzo, L.,Christianson, D.W. (登録日: 2008-10-03, 公開日: 2008-10-21, 最終更新日: 2023-09-06)

主引用文献

Butts, C.A.,Swift, J.,Kang, S.G.,Di Costanzo, L.,Christianson, D.W.,Saven, J.G.,Dmochowski, I.J.
Directing noble metal ion chemistry within a designed ferritin protein.
Biochemistry, 47:12729-12739, 2008

PubMed Abstract: Human H ferritin (HuHF) assembles from 24 four-helix bundles to form an approximately 500 kDa protein with an 8 nm internal cavity. HuHF provides a useful model for studying the transport of metal ions in solution to buried reaction sites in proteins. In this study, HuHF was redesigned to facilitate noble metal ion (Au(3+), Ag(+)) binding, reduction, and nanoparticle formation within the cavity. Computationally determined amino acid substitutions were targeted at four external and four internal surface sites. A variant with a total of 96 cysteines and histidines removed from the exterior surface and 96 non-native cysteines added to the interior surface retained wild-type stability and structure, as confirmed by X-ray crystallography, and promoted the formation of silver or gold nanoparticles within the protein cavity. Crystallographic studies with HuHF variants provide insight into how ferritins control access of metal ions to interior residues that perform chemistry.

PubMed: 18991401
DOI: 10.1021/bi8016735

実験手法

X-RAY DIFFRACTION (2.795 Å)