1Q1F

Crystal structure of murine neuroglobin

1Q1F の概要

• エントリーDOI: 10.2210/pdb1q1f/pdb
• 分子名称: Neuroglobin, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: globin fold, heme protein, neuroglobin, oxygen storage-transport complex, oxygen storage/transport
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17640.78

構造登録者

Vallone, B.,Nienhaus, K.,Matthes, K.,Brunori, M.,Nienhaus, G.U. (登録日: 2003-07-19, 公開日: 2004-06-08, 最終更新日: 2024-02-14)

主引用文献

Vallone, B.,Nienhaus, K.,Brunori, M.,Nienhaus, G.U.
The structure of murine neuroglobin: Novel pathways for ligand migration and binding.
Proteins, 56:85-92, 2004

PubMed Abstract: Neuroglobin, a recently discovered globin predominantly expressed in neuronal tissue of vertebrates, binds small, gaseous ligands at the sixth coordination position of the heme iron. In the absence of an exogenous ligand, the distal histidine (His64) binds to the heme iron in the ferrous and ferric states. The crystal structure of murine ferric (met) neuroglobin at 1.5 A reveals interesting features relevant to the ligand binding mechanism. Only weak selectivity is observed for the two possible heme orientations, the occupancy ratio being 70:30. Two small internal cavities are present on the heme distal side, which enable the His64(E7) side chain to move out of the way upon exogenous ligand binding. Moreover, a third, huge cavity (volume approximately 290 A3) connecting both sides of the heme, is open towards the exterior and provides a potential passageway for ligands. The CD and EF corners exhibit substantial flexibility, which may assist ligands in entering the protein and accessing the active site. Based on this high-resolution structure, further structure-function studies can be planned to elucidate the role of neuroglobin in physiological responses to hypoxia.

PubMed: 15162488
DOI: 10.1002/prot.20113

実験手法

X-RAY DIFFRACTION (1.5 Å)