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  Structural, Biochemical and Genetic Characterization of Dissimilatory ATP Sulfurylase from Allochromatium vinosum

Parey, K., Demmer, U., Warkentin, E., Wynen, A., Ermler, U., & Dahl, C. (2013). Structural, Biochemical and Genetic Characterization of Dissimilatory ATP Sulfurylase from Allochromatium vinosum. PLoS One, 8(9), e74707-e74707. doi:10.1371/journal.pone.0074707.

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Parey, Kristian1, 2, Autor           
Demmer, Ulrike1, Autor                 
Warkentin, Eberhard1, Autor           
Wynen, Astrid3, Autor
Ermler, Ulrich1, Autor                 
Dahl, Christiane3, Autor
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Regensburg, Germany, ou_persistent22              
3Institut für Mikrobiologie & Biotechnologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Bonn, Germany, ou_persistent22              

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 Zusammenfassung: ATP sulfurylase (ATPS) catalyzes a key reaction in the global sulfur cycle by reversibly converting inorganic sulfate (SO42-) with ATP to adenosine 59-phosphosulfate (APS) and pyrophosphate (PPi). In this work we report on the sat encoded dissimilatory ATP sulfurylase from the sulfur-oxidizing purple sulfur bacterium Allochromatium vinosum. In this organism, the sat gene is located in one operon and co-transcribed with the aprMBA genes for membrane-bound APS reductase. Like APS reductase, Sat is dispensible for growth on reduced sulfur compounds due to the presence of an alternate, so far unidentified sulfite-oxidizing pathway in A. vinosum. Sulfate assimilation also proceeds independently of Sat by a separate pathway involving a cysDN-encoded assimilatory ATP sulfurylase. We produced the purple bacterial sat-encoded ATP sulfurylase as a recombinant protein in E. coli, determined crucial kinetic parameters and obtained a crystal structure in an open state with a ligand-free active site. By comparison with several known structures of the ATPS-APS complex in the closed state a scenario about substrate-induced conformational changes was worked out. Despite different kinetic properties ATPS involved in sulfur-oxidizing and sulfate-reducing processes are not distinguishable on a structural level presumably due to the interference between functional and evolutionary processes.

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Sprache(n): eng - English
 Datum: 2013-05-032013-08-042013-09-20
 Publikationsstatus: Erschienen
 Seiten: 9
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1371/journal.pone.0074707
 Art des Abschluß: -

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Titel: PLoS One
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: San Francisco, CA : Public Library of Science
Seiten: - Band / Heft: 8 (9) Artikelnummer: - Start- / Endseite: e74707 - e74707 Identifikator: ISSN: 1932-6203
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000277850