3v17: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of the Fe(II)/alpha-ketoglutarate dependent taurine dioxygenase from Pseudomonas putida KT2440== | ==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=''> | <StructureSection load='3v17' size='340' side='right' caption='[[3v17]], [[Resolution|resolution]] 2.57Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3v17]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3v17]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Psepk Psepk]. 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> | </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='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 | <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 PSEPK])</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='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> | <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://pdbe.org/3v17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3v17 RCSB], [http://www.ebi.ac.uk/pdbsum/3v17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3v17 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 17: | Line 18: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3v17" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
| Line 24: | Line 26: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Psepk]] | ||
[[Category: Taurine dioxygenase]] | [[Category: Taurine dioxygenase]] | ||
[[Category: Dobbek, H]] | [[Category: Dobbek, H]] | ||
Revision as of 15:51, 4 August 2016
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
|
| ||||||||||||||||||||||