2bkm
From Proteopedia
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CRYSTAL STRUCTURE OF THE TRUNCATED HEMOGLOBIN FROM GEOBACILLUS STEAROTHERMOPHILUS
Overview
A novel truncated hemoglobin has been identified in the thermophilic, bacterium Geobacillus stearothermophilus (Gs-trHb). The protein has been, expressed in Escherichia coli, the 3D crystal structure (at 1.5 Angstroms, resolution) and the ligand binding properties have been determined. The, distal heme pocket displays an array of hydrogen bonding donors to the, iron-bound ligands, including Tyr-B10 on one side of the heme pocket and, Trp-G8 indole nitrogen on the opposite side. At variance with the highly, similar Bacillus subtilis hemoglobin, Gs-trHb is dimeric both in the, crystal and in solution and displays several unique structural properties., In the crystal cell, the iron-bound ligand is not homogeneously, distributed within each distal site such that oxygen and an acetate anion, ... [(full description)]
About this Structure
2BKM is a [Single protein] structure of sequence from [Bacillus stearothermophilus] with ACT, OXY and HEM as [ligands]. Full crystallographic information is available from [OCA].
Reference
Crystal structure and ligand binding properties of the truncated hemoglobin from Geobacillus stearothermophilus., Ilari A, Kjelgaard P, von Wachenfeldt C, Catacchio B, Chiancone E, Boffi A, Arch Biochem Biophys. 2007 Jan 1;457(1):85-94. Epub 2006 Oct 30. PMID:17126283
Page seeded by OCA on Mon Oct 29 21:33:23 2007
