2ZA7

recombinant horse L-chain apoferritin N-terminal deletion mutant (residues 1-4)

2ZA7 の概要

• エントリーDOI: 10.2210/pdb2za7/pdb
• 関連するPDBエントリー: 2ZA6 2ZA8
• 分子名称: Ferritin light chain (2 entities in total)
• 機能のキーワード: ferric iron binding, acetylation, iron storage, metal-binding, metal binding protein
• 由来する生物種: Equus caballus (horse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19554.10

構造登録者

Yamashita, I.,Mishima, Y.,Park, S.-Y.,Heddle, J.G.,Tame, J.R.H. (登録日: 2007-10-02, 公開日: 2008-01-22, 最終更新日: 2023-11-01)

主引用文献

Yoshizawa, K.,Mishima, Y.,Park, S.-Y.,Heddle, J.G.,Tame, J.R.H.,Iwahori, K.,Kobayashi, M.,Yamashita, I.
Effect of N-terminal Residues on the Structural Stability of Recombinant Horse L-chain Apoferritin in an Acidic Environment
J.BIOCHEM.(TOKYO), 142:707-713, 2007

PubMed Abstract: The denaturation of recombinant horse L-chain apoferritin (rLF), which is composed of 24 L-chain subunits, in acidic solution was studied. Using two rLF mutants, lacking four (Fer4) or eight (Fer8) N-terminal amino acid residues, the effect of N-terminal residues on the protein's stability was investigated. Of the two mutants and wild-type rLF, the tertiary and secondary structures of Fer8 were found to be most sensitive to an acidic environment. The Fer8 protein dissociated easily into subunit dimers at or below pH 2.0. Comparing the crystal structures of the mutant proteins, deletion of the N-terminal residues was found to result in fewer inter- and intra-subunit hydrogen bonds. The loss of these bonds is assumed to be responsible for lower endurance against acidic denaturation in N-terminus-deleted mutants. These results indicated that the inter- and intra-subunit hydrogen bonds of N-terminal residues affect the denaturation, especially oligomer formation of apoferritin subunits and will be of use in designing ferritin-based nanodevices.

PubMed: 17938140
DOI: 10.1093/jb/mvm187

実験手法

X-RAY DIFFRACTION (1.4 Å)