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Crystal structure and ligand binding properties of the truncated hemoglobin from Geobacillus stearothermophilus

Ilari, Andrea; Kjelgaard, Peter LU ; von Wachenfeldt, Claes LU ; Catacchio, Bruno; Chiancone, Emilia and Boffi, Alberto (2007) In Archives of Biochemistry and Biophysics 457(1). p.85-94
Abstract
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 angstrom 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... (More)
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 angstrom 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 can be resolved with relative occupancies of 50% each. Accordingly, equilibrium titrations of the oxygenated derivative in solution with acetate anion yield a partially saturated ferric acetate adduct. Moreover, the asymmetric unit contains two subunits and sedimentation velocity ultracentrifugation data confirm that the protein is dimeric. (c) 2006 Elsevier Inc. All rights reserved. (Less)
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author
organization
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type
Contribution to journal
publication status
published
subject
keywords
hemoglobin structure, heme ligand binding, thermostable hemoglobins, bacterial hemoglobins, truncated hemoglobins, Geobacillus, stearothermophilus
in
Archives of Biochemistry and Biophysics
volume
457
issue
1
pages
85 - 94
publisher
Academic Press
external identifiers
  • wos:000243311600010
  • scopus:33845699407
ISSN
0003-9861
DOI
10.1016/j.abb.2006.09.033
language
English
LU publication?
yes
id
fb7f9cef-9a38-434b-b153-bc46289aedcd (old id 679824)
date added to LUP
2007-12-11 13:07:09
date last changed
2017-01-01 05:08:31
@article{fb7f9cef-9a38-434b-b153-bc46289aedcd,
  abstract     = {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 angstrom 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 can be resolved with relative occupancies of 50% each. Accordingly, equilibrium titrations of the oxygenated derivative in solution with acetate anion yield a partially saturated ferric acetate adduct. Moreover, the asymmetric unit contains two subunits and sedimentation velocity ultracentrifugation data confirm that the protein is dimeric. (c) 2006 Elsevier Inc. All rights reserved.},
  author       = {Ilari, Andrea and Kjelgaard, Peter and von Wachenfeldt, Claes and Catacchio, Bruno and Chiancone, Emilia and Boffi, Alberto},
  issn         = {0003-9861},
  keyword      = {hemoglobin structure,heme ligand binding,thermostable hemoglobins,bacterial hemoglobins,truncated hemoglobins,Geobacillus,stearothermophilus},
  language     = {eng},
  number       = {1},
  pages        = {85--94},
  publisher    = {Academic Press},
  series       = {Archives of Biochemistry and Biophysics},
  title        = {Crystal structure and ligand binding properties of the truncated hemoglobin from Geobacillus stearothermophilus},
  url          = {http://dx.doi.org/10.1016/j.abb.2006.09.033},
  volume       = {457},
  year         = {2007},
}