1OS7

Crystal structure of TauD with iron, alpha-ketoglutarate and Taurine bound at pH 7.5

Summary for 1OS7

• Entry DOI: 10.2210/pdb1os7/pdb
• Related: 1GQW 1GY9
• Descriptor: Alpha-ketoglutarate-dependent taurine dioxygenase, FE (II) ION, 2-AMINOETHANESULFONIC ACID, ... (5 entities in total)
• Functional Keywords: iron di-oxygenase, taurine, taud, alpha-ketoglutarate, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 130997.08

Authors

O'Brien, J.R.,Schuller, D.J.,Yang, V.S.,Dillard, B.D.,Lanzilotta, W.N. (deposition date: 2003-03-18, release date: 2003-09-23, Last modification date: 2024-02-14)

Primary citation

O'Brien, J.R.,Schuller, D.J.,Yang, V.S.,Dillard, B.D.,Lanzilotta, W.N.
Substrate-Induced Conformational Changes in Escherichia coli Taurine/alpha-Ketoglutarate Dioxygenase and Insight Into the Oligomeric Structure
Biochemistry, 42:5547-5554, 2003

PubMed Abstract: The enzymes in the alpha-ketoglutarate (alphaKG) dependent dioxygenase superfamily represent the largest class of non-heme iron oxidases and have important medical, ecological, and biotechnological roles. One such enzyme, taurine/alpha-ketoglutarate dioxygenase (TauD), catalyzes the conversion of 2-aminoethanesulfonate (taurine) to sulfite and aminoacetaldehyde while decomposing alphaKG to succinate and CO(2). This alphaKG dependent dioxygenase is expressed in Escherichia coli under sulfur starvation conditions and allows the cell to utilize taurine, and other similar sulfonates in the environment, as an alternative sulfur source. In this work, we report the structures of the apo and holo forms of TauD to 1.9 A resolution (R(cryst) = 21.2%, R(free) = 24.9%) and 2.5 A resolution (R(cryst) = 22.5%, R(free) = 27.8%), respectively. The models reported herein provide significant new insight into the substrate orientations at the active site and the conformational changes that are induced upon taurine binding. Furthermore, analysis of our crystallographic data coupled with reanalysis of the crystallographic model (resolution = 3.0 A, R(cryst) = 28.1, R(free) = 32.0) presented by Elkins et al. (Biochemistry (2002) 41, 5185-5192) reveals an alternative oligomeric arrangement for the enzyme that is consistent with the conserved primary and secondary structure elements of other alphaKG dependent dioxygenases.

PubMed: 12741810
DOI: 10.1021/bi0341096

Experimental method

X-RAY DIFFRACTION (2.5 Å)