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The sulfur oxygenase reductase from Acidianus ambivalens is an icosatetramer as shown by crystallization and Patterson analysis.

Urich, Tim ; Coelho, Ricardo ; Kletzin, Arnulf ; Frazão, Carlos (2005)
The sulfur oxygenase reductase from Acidianus ambivalens is an icosatetramer as shown by crystallization and Patterson analysis.
In: Biochimica et biophysica acta, 1747 (2)
Artikel, Bibliographie

Kurzbeschreibung (Abstract)

The sulfur oxygenase reductase (SOR) is the initial enzyme in the aerobic sulfur metabolism of the thermoacidophilic and chemolithoautotrophic crenarchaeote Acidianus ambivalens. Single colorless polyhedral crystals were obtained under two crystallization conditions from SOR preparations heterologously overproduced in Escherichia coli. They belonged to space-group I4 and diffraction data were collected up to 1.7 A resolution. Their Patterson symmetry shows additional 4-, 3- and 2-fold non-crystallographic symmetry rotation axes, characteristic of the point group 432. Taking into account the molecular mass of SOR, the crystal unit cell volume, the non-crystallographic symmetry operators and previous electron microscopy studies of the SOR, it was deduced that the quaternary structure of the functionally active enzyme is an icosatetramer with 871 kDa molecular mass.

Typ des Eintrags: Artikel
Erschienen: 2005
Autor(en): Urich, Tim ; Coelho, Ricardo ; Kletzin, Arnulf ; Frazão, Carlos
Art des Eintrags: Bibliographie
Titel: The sulfur oxygenase reductase from Acidianus ambivalens is an icosatetramer as shown by crystallization and Patterson analysis.
Sprache: Englisch
Publikationsjahr: 2005
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Biochimica et biophysica acta
Jahrgang/Volume einer Zeitschrift: 1747
(Heft-)Nummer: 2
Kurzbeschreibung (Abstract):

The sulfur oxygenase reductase (SOR) is the initial enzyme in the aerobic sulfur metabolism of the thermoacidophilic and chemolithoautotrophic crenarchaeote Acidianus ambivalens. Single colorless polyhedral crystals were obtained under two crystallization conditions from SOR preparations heterologously overproduced in Escherichia coli. They belonged to space-group I4 and diffraction data were collected up to 1.7 A resolution. Their Patterson symmetry shows additional 4-, 3- and 2-fold non-crystallographic symmetry rotation axes, characteristic of the point group 432. Taking into account the molecular mass of SOR, the crystal unit cell volume, the non-crystallographic symmetry operators and previous electron microscopy studies of the SOR, it was deduced that the quaternary structure of the functionally active enzyme is an icosatetramer with 871 kDa molecular mass.

Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie > Sulfur Biochemistry and Microbial Bioenergetics
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10 Fachbereich Biologie
Hinterlegungsdatum: 24 Mai 2011 08:43
Letzte Änderung: 19 Apr 2016 13:19
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