2bkm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==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, 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.
+
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 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.
==About this Structure==
==About this Structure==
Line 17: Line 17:
[[Category: Ilari, A.]]
[[Category: Ilari, A.]]
[[Category: Kjelgaard, P.]]
[[Category: Kjelgaard, P.]]
-
[[Category: Wachenfeldt, C.Von.]]
+
[[Category: Wachenfeldt, C Von.]]
[[Category: ACT]]
[[Category: ACT]]
[[Category: HEM]]
[[Category: HEM]]
Line 26: Line 26:
[[Category: transport]]
[[Category: transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:25:10 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:38:48 2008''

Revision as of 14:38, 21 February 2008


2bkm, resolution 1.50Å

Drag the structure with the mouse to rotate

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 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.

About this Structure

2BKM is a Single protein structure of sequence from Geobacillus stearothermophilus with , and as ligands. Known structural/functional Site: . 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 Thu Feb 21 16:38:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools