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Título

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

Autor Müller, Ilka; Kahnert, Antje; Pape, Thomas; Sheldrick, George M.; Meyer-Klaucke, Wolfram; Dierks, Thomas; Kertesz, Michael; Usón, Isabel
Fecha de publicación 27-feb-2004
EditorAmerican Chemical Society
Citación Biochemistry 43(11): 3075-3088 (2004)
ResumenThe alkylsulfatase AtsK from Pseudomonas putida S-313 belongs to the widespread and versatile non-heme iron(II) α-ketoglutarate-dependent dioxygenase superfamily and catalyzes the oxygenolytic cleavage of a variety of different alkyl sulfate esters to the corresponding aldehyde and sulfate. The enzyme is only expressed under sulfur starvation conditions, providing a selective advantage for bacterial growth in soils and rhizosphere. Here we describe the crystal structure of AtsK in the apo form and in three complexes: with the cosubstrate α-ketoglutarate, with α-ketoglutarate and iron, and finally with α-ketoglutarate, iron, and an alkyl sulfate ester used as substrate in catalytic studies. The overall fold of the enzyme is closely related to that of the taurine/α-ketoglutarate dioxygenase TauD and is similar to the fold observed for other members of the enzyme superfamily. From comparison of these structures with the crystal structure of AtsK and its complexes, we propose a general mechanism for the catalytic cycle of the α-ketoglutarate-dependent dioxygenase superfamily.
Versión del editorhttp://dx.doi.org/10.1021/bi035752v
URI http://hdl.handle.net/10261/113884
DOI10.1021/bi035752v
Identificadoresdoi: 10.1021/bi035752v
issn: 0006-2960
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