1gdl
From Proteopedia
|
CRYSTAL STRUCTURE OF FERRIC COMPLEXES OF THE YELLOW LUPIN LEGHEMOGLOBIN WITH ISOQUINOLINE AT 1.8 ANGSTROMS RESOLUTION (RUSSIAN)
Overview
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.
About this Structure
1GDL is a Single protein structure of sequence from Lupinus luteus with HEM and NO as ligands. Full crystallographic information is available from OCA.
Reference
The binding of carbon monoxide and nitric oxide to leghaemoglobin in comparison with other haemoglobins., Harutyunyan EH, Safonova TN, Kuranova IP, Popov AN, Teplyakov AV, Obmolova GV, Valnshtein BK, Dodson GG, Wilson JC, J Mol Biol. 1996 Nov 22;264(1):152-61. PMID:8950274
Page seeded by OCA on Thu Nov 8 13:03:18 2007
