Crystal Structure of the Alkylsulfatase AtsK: Insights into the Catalytic Mechanism of the Fe(II) -Ketoglutarate-Dependent Dioxygena

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• 作者：Ilka M&uuml ; ller ; Antje Kahnert ; Thomas Pape ; George M. Sheldrick ; Wolfram Meyer-Klaucke ; Thomas Dierks ; Michael Kertesz ; and Isabel Usó ; n^$
• 刊名：Biochemistry
• 出版年：2004
• 出版时间：March 23, 2004
• 年：2004
• 卷：43
• 期：11
• 页码：3075 - 3088
• 全文大小：884K
• 年卷期：v.43,no.11(March 23, 2004)
• ISSN：1520-4995

文摘

The alkylsulfatase AtsK from Pseudomonas putida S-313 belongs to the widespread and versatilenon-heme iron(II) mages/gifchars/alpha.gif" BORDER=0>-ketoglutarate-dependent dioxygenase superfamily and catalyzes the oxygenolyticcleavage of a variety of different alkyl sulfate esters to the corresponding aldehyde and sulfate. The enzymeis only expressed under sulfur starvation conditions, providing a selective advantage for bacterial growthin soils and rhizosphere. Here we describe the crystal structure of AtsK in the apo form and in threecomplexes: with the cosubstrate mages/gifchars/alpha.gif" BORDER=0>-ketoglutarate, with mages/gifchars/alpha.gif" BORDER=0>-ketoglutarate and iron, and finally withmages/gifchars/alpha.gif" BORDER=0>-ketoglutarate, iron, and an alkyl sulfate ester used as substrate in catalytic studies. The overall fold ofthe enzyme is closely related to that of the taurine/mages/gifchars/alpha.gif" BORDER=0>-ketoglutarate dioxygenase TauD and is similar to thefold observed for other members of the enzyme superfamily. From comparison of these structures withthe crystal structure of AtsK and its complexes, we propose a general mechanism for the catalytic cycleof the mages/gifchars/alpha.gif" BORDER=0>-ketoglutarate-dependent dioxygenase superfamily.