1gqw

From Proteopedia

Revision as of 13:12, 30 October 2007

TAURINE/ALPHA-KETOGLUTARATE DIOXYGENASE FROM ESCHERICHIA COLI

Overview

Taurine/alpha-ketoglutarate dioxygenase (TauD), a non-heme Fe(II), oxygenase, catalyses the conversion of taurine (2-aminoethanesulfonate) to, sulfite and aminoacetaldehyde concurrent with the conversion of, alpha-ketoglutarate (alphaKG) to succinate and CO(2). The enzyme allows, Escherichia coli to use taurine, widely available in the environment, as, an alternative sulfur source. Here we describe the X-ray crystal structure, of TauD complexed to Fe(II) and both substrates, alphaKG and taurine. The, tertiary structure and fold of TauD are similar to those observed in other, enzymes from the broad family of Fe(II)/alphaKG-dependent oxygenases, with, closest structural similarity to clavaminate synthase. Using the TauD, coordinates, a model was determined for the closely related enzyme, ... [(full description)]

About this Structure

1GQW is a [Single protein] structure of sequence from [Escherichia coli] with FE2, TAU and AKG as [ligands]. Active as [Taurine dioxygenase], with EC number [1.14.11.17]. Structure known Active Site: FEA. Full crystallographic information is available from [OCA].

Reference

X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates., Elkins JM, Ryle MJ, Clifton IJ, Dunning Hotopp JC, Lloyd JS, Burzlaff NI, Baldwin JE, Hausinger RP, Roach PL, Biochemistry. 2002 Apr 23;41(16):5185-92. PMID:11955067

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