1gqw: Difference between revisions
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==Overview== | ==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, ... | 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, 2,4-dichlorophenoxyacetate/alphaKG dioxygenase (TfdA), supporting, predictions derived from site-directed mutagenesis and other studies of, that biodegradative protein. The TauD structure and TfdA model define the, metal ligands and the positions of nearby aromatic residues that undergo, post-translational modifications involving self-hydroxylation reactions., The substrate binding residues of TauD were identified and those of TfdA, predicted. These results, along with sequence alignment information, reveal how TauD selects a tetrahedral substrate anion in preference to the, planar carboxylate selected by TfdA, providing insight into the mechanism, of enzyme catalysis. | ||
==About this Structure== | ==About this Structure== | ||
1GQW is a | 1GQW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with FE2, TAU and AKG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Taurine_dioxygenase Taurine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.17 1.14.11.17] Structure known Active Site: FEA. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GQW OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: tfda]] | [[Category: tfda]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:32:26 2007'' | ||
