1oii
From Proteopedia
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CRYSTAL STRUCTURE OF THE ALKYLSULFATASE ATSK, A NON-HEME FE(II) ALPHAKETOGLUTARATE DEPENDENT DIOXYGENASE IN COMPLEX WITH IRON AND ALPHAKETOGLUTARATE
Overview
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.
About this Structure
1OII is a Single protein structure of sequence from Pseudomonas putida with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of the alkylsulfatase AtsK: insights into the catalytic mechanism of the Fe(II) alpha-ketoglutarate-dependent dioxygenase superfamily., Muller I, Kahnert A, Pape T, Sheldrick GM, Meyer-Klaucke W, Dierks T, Kertesz M, Uson I, Biochemistry. 2004 Mar 23;43(11):3075-88. PMID:15023059
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