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| | <StructureSection load='1gy9' size='340' side='right'caption='[[1gy9]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1gy9' size='340' side='right'caption='[[1gy9]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gy9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GY9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gy9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GY9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=TAU:2-AMINOETHANESULFONIC+ACID'>TAU</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gqw|1gqw]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=TAU:2-AMINOETHANESULFONIC+ACID'>TAU</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Taurine_dioxygenase Taurine dioxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.17 1.14.11.17] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gy9 OCA], [https://pdbe.org/1gy9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gy9 RCSB], [https://www.ebi.ac.uk/pdbsum/1gy9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gy9 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gy9 OCA], [https://pdbe.org/1gy9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gy9 RCSB], [https://www.ebi.ac.uk/pdbsum/1gy9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gy9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TAUD_ECOLI TAUD_ECOLI] Catalyzes the conversion of taurine and alpha ketoglutarate to sulfite, aminoacetaldehyde and succinate. Required for the utilization of taurine (2-aminoethanesulfonic acid) as an alternative sulfur source. Pentane-sulfonic acid, 3-(N-morpholino)propanesulfonic acid and 1,3-dioxo-2-isoindolineethanesulfonic acid are also substrates for this enzyme. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Taurine dioxygenase]]
| + | [[Category: Baldwin JE]] |
| - | [[Category: Baldwin, J E]] | + | [[Category: Burzlaff NI]] |
| - | [[Category: Burzlaff, N I]] | + | [[Category: Clifton IJ]] |
| - | [[Category: Clifton, I J]] | + | [[Category: Elkins JM]] |
| - | [[Category: Elkins, J M]] | + | [[Category: Hausinger RP]] |
| - | [[Category: Hausinger, R P]] | + | [[Category: Lloyd JS]] |
| - | [[Category: Lloyd, J S]] | + | [[Category: Roach PL]] |
| - | [[Category: Roach, P L]] | + | [[Category: Ryle MJ]] |
| - | [[Category: Ryle, M J]] | + | |
| - | [[Category: Alpha-ketoglutarate]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Oxygenase]]
| + | |
| - | [[Category: Sulphur metabolism]]
| + | |
| - | [[Category: Taud]]
| + | |
| - | [[Category: Taurine]]
| + | |
| - | [[Category: Tfda]]
| + | |
| Structural highlights
Function
TAUD_ECOLI Catalyzes the conversion of taurine and alpha ketoglutarate to sulfite, aminoacetaldehyde and succinate. Required for the utilization of taurine (2-aminoethanesulfonic acid) as an alternative sulfur source. Pentane-sulfonic acid, 3-(N-morpholino)propanesulfonic acid and 1,3-dioxo-2-isoindolineethanesulfonic acid are also substrates for this enzyme.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Elkins JM, Ryle MJ, Clifton IJ, Dunning Hotopp JC, Lloyd JS, Burzlaff NI, Baldwin JE, Hausinger RP, Roach PL. X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates. Biochemistry. 2002 Apr 23;41(16):5185-92. PMID:11955067
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