Crystal structure and ligand binding properties of the truncated hemoglobin from Geobacillus stearothermophilus. (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Crystal structure and ligand binding properties of the truncated hemoglobin from Geobacillus stearothermophilus. (Articolo in rivista) (literal)

Anno

• 2007-01-01T00:00:00+01:00 (literal)

Alternative label

• Ilari A, Kjelgaard P, von Wachenfeldt C, Catacchio B, Chiancone E, Boffi A. (2007)
  Crystal structure and ligand binding properties of the truncated hemoglobin from Geobacillus stearothermophilus.
  in Archives of biochemistry and biophysics (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Ilari A, Kjelgaard P, von Wachenfeldt C, Catacchio B, Chiancone E, Boffi A. (literal)

Pagina inizio

• 85 (literal)

Pagina fine

• 94 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 457 (literal)

Rivista

• Archives of biochemistry and biophysics (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• 1. Univ Roma La Sapienza, Dept Biochem Sci, I-00185 Rome, Italy 2. Univ Roma La Sapienza, CNR, Inst Mol Biol & Pathol, I-00185 Rome, Italy 3. Lund Univ, Dept Cell & Organism Biol, SE-22362 Lund, Sweden (literal)

Titolo

• Crystal structure and ligand binding properties of the truncated hemoglobin from Geobacillus stearothermophilus. (literal)

Abstract

• 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. (literal)

Prodotto di

• Biologia strutturale e bioinformatica: struttura-funzione, dinamica e riconoscimento in proteine (SV.P14.008.001) (Modulo)
• Institute of molecular biology and pathology (IBPM) (Istituto)

Autore CNR

• EMILIA CHIANCONE (Unità di personale esterno)
• ANDREA ILARI (Unità di personale interno)
• ALBERTO BOFFI (Unità di personale esterno)

Incoming links:

Prodotto

• Institute of molecular biology and pathology (IBPM) (Istituto)
• Biologia strutturale e bioinformatica: struttura-funzione, dinamica e riconoscimento in proteine (SV.P14.008.001) (Modulo)

Autore CNR di

• EMILIA CHIANCONE (Unità di personale esterno)
• ANDREA ILARI (Unità di personale interno)
• ALBERTO BOFFI (Unità di personale esterno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Archives of biochemistry and biophysics (Rivista)