6I3T
Crystal structure of murine neuroglobin bound to CO at 40 K.
6I3T の概要
エントリーDOI | 10.2210/pdb6i3t/pdb |
分子名称 | Neuroglobin, PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE, ... (7 entities in total) |
機能のキーワード | oxygen transport/storage, carbon monoxide, photodissociation, oxygen transport |
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 | 18098.12 |
構造登録者 | Savino, C.,Montemiglio, L.C.,Ardiccioni, C.,Exertier, C. (登録日: 2018-11-07, 公開日: 2019-09-11, 最終更新日: 2024-01-24) |
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 Cited by 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: 31576217DOI: 10.1107/S2052252519008157 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード
