6BB5

Human Oxy-Hemoglobin

6BB5 の概要

• エントリーDOI: 10.2210/pdb6bb5/pdb
• 関連するPDBエントリー: 2DN1 5WOG 5WOH
• 分子名称: Hemoglobin subunit alpha, Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• 機能のキーワード: hemoglobin, oxygen, r-state, oxygen transport
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31982.07

構造登録者

Gumpper, R.H.,Terrell, J.R.,Luo, M. (登録日: 2017-10-16, 公開日: 2018-01-10, 最終更新日: 2023-10-04)

主引用文献

Terrell, J.R.,Gumpper, R.H.,Luo, M.
Hemoglobin crystals immersed in liquid oxygen reveal diffusion channels.
Biochem. Biophys. Res. Commun., 495:1858-1863, 2018

PubMed Abstract: Human hemoglobin (HbA) transports molecular oxygen (O) from the lung to tissues where the partial pressure of O is lower. O binds to HbA at the heme cofactor and is stabilized by a distal histidine (HisE7). HisE7 has been observed to occupy opened and closed conformations, and is postulated to act as a gate controlling the binding/release of O. However, it has been suggested that HbA also contains intraprotein oxygen channels for entrances/exits far from the heme. In this study, we developed a novel method of crystal immersion in liquid oxygen prior to X-ray data collection. In the crystals immersed in liquid oxygen, the heme center was oxidized to generate aquomethemoglobin. Increases of structural flexibility were also observed in regions that are synonymous with previously postulated oxygen channels. These regions also correspond to medically relevant mutations which affect O affinity. The way HbA utilizes these O channels could have a profound impact on understanding the relationship of HbA O transport within these disease conditions. Finally, the liquid oxygen immersion technique can be utilized as a new tool to crystallographically examine proteins and protein complexes which utilize O for enzyme catalysis or transport.

PubMed: 29246762
DOI: 10.1016/j.bbrc.2017.12.038

実験手法

X-RAY DIFFRACTION (2.28 Å)