1OII

Crystal structure of the alkylsulfatase AtsK, a non-heme Fe(II) alphaketoglutarate dependent Dioxygenase in complex with iron and alphaketoglutarate

Summary for 1OII

• Entry DOI: 10.2210/pdb1oii/pdb
• Related: 1OIH 1OIJ 1OIK
• Descriptor: PUTATIVE ALKYLSULFATASE ATSK, FE (II) ION, 2-OXOGLUTARIC ACID, ... (4 entities in total)
• Functional Keywords: jelly roll, oxidoreductase
• Biological source: PSEUDOMONAS PUTIDA
• Total number of polymer chains: 4
• Total formula weight: 133801.38

Authors

Mueller, I.,Kahnert, A.,Pape, T.,Dierks, T.,Meyer-Klauke, W.,Kertesz, M.A.,Uson, I. (deposition date: 2003-06-18, release date: 2004-03-30, Last modification date: 2023-12-13)

Primary citation

Mueller, I.,Kahnert, A.,Pape, T.,Sheldrick, G.M.,Meyer-Klaucke, W.,Dierks, T.,Kertesz, M.A.,Uson, I.
Crystal Structure of the Alkylsulfatase Atsk: Insights Into the Catalytic Mechanism of the Fe(II) Alpha-Ketoglutarate-Dependent Dioxygenase Superfamily
Biochemistry, 42:3075-, 2004

PubMed Abstract: The alkylsulfatase AtsK from Pseudomonas putida S-313 belongs to the widespread and versatile non-heme iron(II) alpha-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 alpha-ketoglutarate, with alpha-ketoglutarate and iron, and finally with alpha-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/alpha-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 alpha-ketoglutarate-dependent dioxygenase superfamily.

PubMed: 15023059
DOI: 10.1021/BI035752V

Experimental method

X-RAY DIFFRACTION (2.19 Å)