5MJC

metNeuroglobin under oxygen at 50 bar

5MJC の概要

• エントリーDOI: 10.2210/pdb5mjc/pdb
• 関連するPDBエントリー: 1OJ6 3gkt 4o4t
• 分子名称: Neuroglobin, PROTOPORPHYRIN IX CONTAINING FE, 1,4-DIETHYLENE DIOXIDE, ... (6 entities in total)
• 機能のキーワード: oxygen complex storage cavity, 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: 17555.63

構造登録者

Prange, T.,Colloc'h, N.,Carpentier, P.,Vallone, B. (登録日: 2016-11-30, 公開日: 2017-12-20, 最終更新日: 2024-01-17)

主引用文献

Ardiccioni, C.,Arcovito, A.,Della Longa, S.,van der Linden, P.,Bourgeois, D.,Weik, M.,Montemiglio, L.C.,Savino, C.,Avella, G.,Exertier, C.,Carpentier, P.,Prange, T.,Brunori, M.,Colloc'h, N.,Vallone, B.
Ligand pathways in neuroglobin revealed by low-temperature photodissociation and docking experiments.
Iucrj, 6:832-842, 2019

PubMed Abstract: A combined biophysical approach was applied to map gas-docking sites within murine neuroglobin (Ngb), revealing snapshots of events that might govern activity and dynamics in this unique hexacoordinate globin, which is most likely to be involved in gas-sensing in the central nervous system and for which a precise mechanism of action remains to be elucidated. The application of UV-visible microspectroscopy , solution X-ray absorption near-edge spectroscopy and X-ray diffraction experiments at 15-40 K provided the structural characterization of an Ngb photolytic intermediate by cryo-trapping and allowed direct observation of the relocation of carbon monoxide within the distal heme pocket after photodissociation. Moreover, X-ray diffraction at 100 K under a high pressure of dioxygen, a physiological ligand of Ngb, unravelled the existence of a storage site for O in Ngb which coincides with Xe-III, a previously described docking site for xenon or krypton. Notably, no other secondary sites were observed under our experimental conditions.

PubMed: 31576217
DOI: 10.1107/S2052252519008157

実験手法

X-RAY DIFFRACTION (1.62 Å)