3GLN

Carbonmonoxy Ngb under Xenon pressure

3GLN の概要

• エントリーDOI: 10.2210/pdb3gln/pdb
• 関連するPDBエントリー: 3GK9 3GKT
• 分子名称: Neuroglobin, SULFATE ION, XENON, ... (6 entities in total)
• 機能のキーワード: neuroglobin, hemeprotein, xenon binding, cavities, oxygen storage-transport protein complex, heme, iron, metal-binding, oxygen transport, transport, oxygen storage/transport protein
• 由来する生物種: Mus musculus (mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18572.30

構造登録者

Moschetti, T.,Mueller, U.,Schultze, J.,Brunori, M.,Vallone, B. (登録日: 2009-03-12, 公開日: 2009-09-22, 最終更新日: 2023-11-01)

主引用文献

Moschetti, T.,Mueller, U.,Schulze, J.,Brunori, M.,Vallone, B.
The structure of neuroglobin at high Xe and Kr pressure reveals partial conservation of globin internal cavities.
Biophys. J., 97:1700-1708, 2009

PubMed Abstract: Neuroglobin (Ngb) is a hexacoordinate globin expressed in the brain of vertebrates. Ferrous Ngb binds dioxygen with high affinity and the O(2) adduct is able to scavenge NO. Convincing in vitro and in vivo data indicate that Ngb is involved in neuroprotection during hypoxia and ischemia. The 3D structure of Ngb reveals the presence of a wide internal cavity connecting its heme active site with the bulk. To explore the role of this "tunnel" in the control of ligand binding, we determined the structure of metNgb and NgbCO equilibrated with Xe or Kr. We show four docking sites for Xe (only two for Kr); two of the four Xe sites are within the large cavity. They are only partially conserved in globins, since the two proximal Xe sites identified in myoglobin (Xe1 and Xe2) are absent in Ngb, as well as in cytoglobin. The Xe docking sites in Ngb map a pathway within the protein matrix, leading to the heme, which becomes more accessible in the ligand-bound species. This may be of significance in connection with the redox chemistry that may be the primary function of this hexacoordinate globin.

PubMed: 19751675
DOI: 10.1016/j.bpj.2009.05.059

実験手法

X-RAY DIFFRACTION (2.26 Å)