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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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資料種別: 学術論文

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 作成者:
Parey, Kristian1, 2, 著者           
Demmer, Ulrike1, 著者                 
Warkentin, Eberhard1, 著者           
Wynen, Astrid3, 著者
Ermler, Ulrich1, 著者                 
Dahl, Christiane3, 著者
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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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 要旨: 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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言語: eng - English
 日付: 2013-05-032013-08-042013-09-20
 出版の状態: 出版
 ページ: 9
 出版情報: -
 目次: -
 査読: 査読あり
 識別子(DOI, ISBNなど): DOI: 10.1371/journal.pone.0074707
 学位: -

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出版物名: PLoS One
種別: 学術雑誌
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出版社, 出版地: San Francisco, CA : Public Library of Science
ページ: - 巻号: 8 (9) 通巻号: - 開始・終了ページ: e74707 - e74707 識別子(ISBN, ISSN, DOIなど): ISSN: 1932-6203
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000277850