1GDL

CRYSTAL STRUCTURE OF FERRIC COMPLEXES OF THE YELLOW LUPIN LEGHEMOGLOBIN WITH ISOQUINOLINE AT 1.8 ANGSTROMS RESOLUTION (RUSSIAN)

1GDL の概要

• エントリーDOI: 10.2210/pdb1gdl/pdb
• 分子名称: LEGHEMOGLOBIN (NITROGEN MONOXY), PROTOPORPHYRIN IX CONTAINING FE, NITRIC OXIDE, ... (4 entities in total)
• 機能のキーワード: oxygen transport
• 由来する生物種: Lupinus luteus (yellow lupine)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17320.56

構造登録者

Harutyunyan, E.,Safonova, T.,Kuranova, I. (登録日: 1994-09-14, 公開日: 1995-02-27, 最終更新日: 2024-02-07)

主引用文献

Harutyunyan, E.H.,Safonova, T.N.,Kuranova, I.P.,Popov, A.N.,Teplyakov, A.V.,Obmolova, G.V.,Valnshtein, B.K.,Dodson, G.G.,Wilson, J.C.
The binding of carbon monoxide and nitric oxide to leghaemoglobin in comparison with other haemoglobins.
J.Mol.Biol., 264:152-161, 1996

PubMed Abstract: Haemoglobins have the ability to discriminate between oxygen and other diatomic molecules. To further understanding of this process the X-ray crystal structures of carbonmonoxy and nitrosyl-leghaemoglobin have been determined at 1.8 A resolution. The ligand geometry is discussed in detail and the controversial issue of bent versus linear carbon monoxide binding is addressed. The bond angle of 160 degrees for CO-leghaemoglobin is in conflict with recent spectroscopy results on myoglobin but is consistent with angles obtained for myoglobin X-ray crystal structures. In contrast to the numerous carbon monoxide studies, very little stereochemical information is available for the nitric oxide adduct of haemoglobin. This is provided by the X-ray structure of NO-leghaemoglobin, which conforms to expected geometry with an Fe-NO angle of 147 degrees and a lengthened iron-proximal histidine bond. Thus crystallographic evidence is given for the predicted weakening of this bond on the binding of nitric oxide.

PubMed: 8950274
DOI: 10.1006/jmbi.1996.0630

実験手法

X-RAY DIFFRACTION (1.8 Å)