3v17: Difference between revisions
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==Crystal structure of the Fe(II)/alpha-ketoglutarate dependent taurine dioxygenase from Pseudomonas putida KT2440== | |||
=== | <StructureSection load='3v17' size='340' side='right' caption='[[3v17]], [[Resolution|resolution]] 2.57Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3v17]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida_kt2440 Pseudomonas putida kt2440]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V17 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pvj|3pvj]], [[3v15|3v15]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PP0230, PP_0230, tauD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160488 Pseudomonas putida KT2440])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3v17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v17 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v17 RCSB], [http://www.ebi.ac.uk/pdbsum/3v17 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Fe(II)/alpha-ketoglutarate dependent oxygenases are versatile catalysts associated with a number of different biological functions, in which they use the oxidizing power of activated dioxygen to convert a variety of substrates. A mononuclear non-heme iron center is used to couple the decarboxylation of the cosubstrate alpha-ketoglutarate with a two-electron oxidation of the substrate, which is a hydroxylation in most cases. Although Fe(II)/alpha-ketoglutarate dependent oxygenases have diverse amino acid sequences and substrate specifity, it is assumed that they share a common mechanism. One representative of this enzyme family is the Fe(II)/alpha-ketoglutarate dependent taurine dioxygenase (TauD) that catalyzes the hydroxylation of taurine yielding sulfite and aminoacetaldehyde. Its mechanism has been studied in detail becoming a model system for the whole enzyme family. However, its oligomeric state and architecture have been disputed. Here, we report the biochemical and kinetic characterization of the Fe(II)/alpha-ketoglutarate dependent taurine dioxygenase from Pseudomonas putida KT2440 (TauD(Pp) ). We also present three crystal structures of the apo form of this enzyme. Comparisons with TauD from Escherichia coli (TauD(Ec) ) demonstrate that both enzymes are quite similar regarding their spectra, structure and kinetics and only minor differences for the accumulation of intermediates during the reaction have been observed. Structural data and the analytical gelfiltration as well as sedimentation velocity analytical ultracentrifugation show that both TauD(Pp) and TauD(Ec) are tetramers in solution and in the crystals, which is in contrast to the earlier description of TauD from E. coli as a dimer. Structured digital abstract tauDpp and tauDpp bind by molecularsieving (Viewinteraction) tauDpp and tauDpp bind by x-raycrystallography (Viewinteraction) tauDEc and tauDEc bind by molecularsieving (Viewinteraction). | |||
The Fe(II) /alpha-ketoglutarate dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers.,Knauer SH, Hartl-Spiegelhauer O, Schwarzinger S, Hanzelmann P, Dobbek H FEBS J. 2012 Jan 5. doi: 10.1111/j.1742-4658.2012.08473.x. PMID:22221834<ref>PMID:22221834</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
==See Also== | |||
*[[Dioxygenase|Dioxygenase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Pseudomonas putida kt2440]] | [[Category: Pseudomonas putida kt2440]] | ||
[[Category: Taurine dioxygenase]] | [[Category: Taurine dioxygenase]] | ||
[[Category: Dobbek, H | [[Category: Dobbek, H]] | ||
[[Category: Knauer, S H | [[Category: Knauer, S H]] | ||
[[Category: Alpha-ketoglutarate]] | [[Category: Alpha-ketoglutarate]] | ||
[[Category: Dioxygenase]] | [[Category: Dioxygenase]] | ||
Revision as of 10:16, 21 December 2014
Crystal structure of the Fe(II)/alpha-ketoglutarate dependent taurine dioxygenase from Pseudomonas putida KT2440Crystal structure of the Fe(II)/alpha-ketoglutarate dependent taurine dioxygenase from Pseudomonas putida KT2440
Structural highlights
Publication Abstract from PubMedFe(II)/alpha-ketoglutarate dependent oxygenases are versatile catalysts associated with a number of different biological functions, in which they use the oxidizing power of activated dioxygen to convert a variety of substrates. A mononuclear non-heme iron center is used to couple the decarboxylation of the cosubstrate alpha-ketoglutarate with a two-electron oxidation of the substrate, which is a hydroxylation in most cases. Although Fe(II)/alpha-ketoglutarate dependent oxygenases have diverse amino acid sequences and substrate specifity, it is assumed that they share a common mechanism. One representative of this enzyme family is the Fe(II)/alpha-ketoglutarate dependent taurine dioxygenase (TauD) that catalyzes the hydroxylation of taurine yielding sulfite and aminoacetaldehyde. Its mechanism has been studied in detail becoming a model system for the whole enzyme family. However, its oligomeric state and architecture have been disputed. Here, we report the biochemical and kinetic characterization of the Fe(II)/alpha-ketoglutarate dependent taurine dioxygenase from Pseudomonas putida KT2440 (TauD(Pp) ). We also present three crystal structures of the apo form of this enzyme. Comparisons with TauD from Escherichia coli (TauD(Ec) ) demonstrate that both enzymes are quite similar regarding their spectra, structure and kinetics and only minor differences for the accumulation of intermediates during the reaction have been observed. Structural data and the analytical gelfiltration as well as sedimentation velocity analytical ultracentrifugation show that both TauD(Pp) and TauD(Ec) are tetramers in solution and in the crystals, which is in contrast to the earlier description of TauD from E. coli as a dimer. Structured digital abstract tauDpp and tauDpp bind by molecularsieving (Viewinteraction) tauDpp and tauDpp bind by x-raycrystallography (Viewinteraction) tauDEc and tauDEc bind by molecularsieving (Viewinteraction). The Fe(II) /alpha-ketoglutarate dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers.,Knauer SH, Hartl-Spiegelhauer O, Schwarzinger S, Hanzelmann P, Dobbek H FEBS J. 2012 Jan 5. doi: 10.1111/j.1742-4658.2012.08473.x. PMID:22221834[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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