4O2G

Crystal structure of carbomonoxy murine neuroglobin mutant V140W

4O2G の概要

• エントリーDOI: 10.2210/pdb4o2g/pdb
• 関連するPDBエントリー: 1W92 4MU5 4NZI 4O1T 4O35
• 分子名称: Neuroglobin, PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE (3 entities in total)
• 機能のキーワード: globin, oxygen storage, transport protein
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Perikaryon (By similarity): Q9ER97
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18038.15

構造登録者

Avella, G.,Savino, C.,Vallone, B. (登録日: 2013-12-17, 公開日: 2014-06-18, 最終更新日: 2024-02-28)

主引用文献

Avella, G.,Ardiccioni, C.,Scaglione, A.,Moschetti, T.,Rondinelli, C.,Montemiglio, L.C.,Savino, C.,Giuffre, A.,Brunori, M.,Vallone, B.
Engineering the internal cavity of neuroglobin demonstrates the role of the haem-sliding mechanism.
Acta Crystallogr.,Sect.D, 70:1640-1648, 2014

PubMed Abstract: Neuroglobin is a member of the globin family involved in neuroprotection; it is primarily expressed in the brain and retina of vertebrates. Neuroglobin belongs to the heterogeneous group of hexacoordinate globins that have evolved in animals, plants and bacteria, endowed with the capability of reversible intramolecular coordination, allowing the binding of small gaseous ligands (O2, NO and CO). In a unique fashion among haemoproteins, ligand-binding events in neuroglobin are dependent on the sliding of the haem itself within a preformed internal cavity, as revealed by the crystal structure of its CO-bound derivative. Point mutants of the neuroglobin internal cavity have been engineered and their functional and structural characterization shows that hindering the haem displacement leads to a decrease in CO affinity, whereas reducing the cavity volume without interfering with haem sliding has negligible functional effects.

PubMed: 24914975
DOI: 10.1107/S1399004714007032

実験手法

X-RAY DIFFRACTION (2.7 Å)