6FQF

THE X-RAY STRUCTURE OF FERRIC-BETA4 HUMAN HEMOGLOBIN

6FQF の概要

• エントリーDOI: 10.2210/pdb6fqf/pdb
• 分子名称: Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: human hemoglobin, oxygen transport
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 66026.74

構造登録者

Mazzarella, L.,Merlino, A.,Balasco, N.,Balsamo, A.,Vergara, A. (登録日: 2018-02-14, 公開日: 2018-06-13, 最終更新日: 2024-10-16)

主引用文献

Mazzarella, L.,Merlino, A.,Balasco, N.,Balsamo, A.,Vergara, A.
Crystal structure of the ferric homotetrameric beta4human hemoglobin.
Biophys. Chem., 240:9-14, 2018

PubMed Abstract: Spectroscopic studies carried out in the early seventies have shown that the β-homotetramer of human hemoglobin (β-HbA) in the ferric state is a mixture of aquomet and bis-histidyl forms. Here we present the first crystal structure, solved at 2.10 Å resolution, of the oxidized form of β-HbA. The overall quaternary structure of the protein in the ferric state is virtually indistinguishable from that of the ferrous deoxygenated and carbomonoxy forms. The structure reveals that the four hemes are exclusively in an aquomet coordination, without any trace of bis-histidyl coordination. The oxidation of β-HbA is associated with the formation of a disulfide bridge between residues Cys112(G14) of β/β and β/β chains. The coordination state of β-HbA has been compared to that known for other organisms that exhibit bis-histidyl heme coordination in the β state. This occurrence has been discussed in terms of different organism physiology.

PubMed: 29857171
DOI: 10.1016/j.bpc.2018.05.003

実験手法

X-RAY DIFFRACTION (2.1 Å)