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| | ==Kinetic and Structural Characterization of a Heterohexamer 4-Oxalocrotonate Tautomerase from Chloroflexus aurantiacus J-10-fl: Implications for Functional and Structural Diversity in the Tautomerase Superfamily== | | ==Kinetic and Structural Characterization of a Heterohexamer 4-Oxalocrotonate Tautomerase from Chloroflexus aurantiacus J-10-fl: Implications for Functional and Structural Diversity in the Tautomerase Superfamily== |
| - | <StructureSection load='3mb2' size='340' side='right' caption='[[3mb2]], [[Resolution|resolution]] 2.41Å' scene=''> | + | <StructureSection load='3mb2' size='340' side='right'caption='[[3mb2]], [[Resolution|resolution]] 2.41Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3mb2]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlaa Chlaa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MB2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3mb2]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Chloroflexus_aurantiacus_J-10-fl Chloroflexus aurantiacus J-10-fl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MB2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.41Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">4-oxalocrotonate tautomerase, Caur_1354 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=324602 CHLAA]), 4-oxalocrotonate tautomerase, Caur_1358 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=324602 CHLAA])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxaloacetate_tautomerase Oxaloacetate tautomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.2.2 5.3.2.2] </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=3mb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mb2 OCA], [https://pdbe.org/3mb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mb2 RCSB], [https://www.ebi.ac.uk/pdbsum/3mb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mb2 ProSAT]</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=3mb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mb2 OCA], [http://pdbe.org/3mb2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mb2 RCSB], [http://www.ebi.ac.uk/pdbsum/3mb2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mb2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A9W9U6_CHLAA A9W9U6_CHLAA] |
| | == 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: Chlaa]] | + | [[Category: Chloroflexus aurantiacus J-10-fl]] |
| - | [[Category: Oxaloacetate tautomerase]] | + | [[Category: Large Structures]] |
| - | [[Category: Burks, E A]] | + | [[Category: Burks EA]] |
| - | [[Category: Fleming, C D]] | + | [[Category: Fleming CD]] |
| - | [[Category: Mesecar, A D]] | + | [[Category: Mesecar AD]] |
| - | [[Category: Pegan, S D]] | + | [[Category: Pegan SD]] |
| - | [[Category: Whitman, C P]] | + | [[Category: Whitman CP]] |
| - | [[Category: 4-ot]]
| + | |
| - | [[Category: 4-oxalocrotonate tautomerase]]
| + | |
| - | [[Category: Caad]]
| + | |
| - | [[Category: Dehalogenase]]
| + | |
| - | [[Category: Heterohexamer]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Trans-3-chloroacrylic acid dehalogenase]]
| + | |
| Structural highlights
Function
A9W9U6_CHLAA
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
4-Oxalocrotonate tautomerase (4-OT) isozymes play prominent roles in the bacterial utilization of aromatic hydrocarbons as sole carbon sources. These enzymes catalyze the conversion of 2-hydroxy-2,4-hexadienedioate (or 2-hydroxymuconate) to 2-oxo-3-hexenedioate, where Pro-1 functions as a general base and shuttles a proton from the 2-hydroxyl group of the substrate to the C-5 position of the product. 4-OT, a homohexamer from Pseudomonas putida mt-2, is the most extensively studied 4-OT isozyme and the founding member of the tautomerase superfamily. A search of five thermophilic bacterial genomes identified a coded amino acid sequence in each that had been annotated as a tautomerase-like protein but lacked Pro-1. However, a nearby sequence has Pro-1, but the sequence is not annotated as a tautomerase-like protein. To characterize this group of proteins, two genes from Chloroflexus aurantiacus J-10-fl were cloned, and the corresponding proteins were expressed. Kinetic, biochemical, and X-ray structural analyses show that the two expressed proteins form a functional heterohexamer 4-OT (hh4-OT), composed of three alphabeta dimers. Like the P. putida enzyme, hh4-OT requires the amino-terminal proline and two arginines for the conversion of 2-hydroxymuconate to the product, implicating an analogous mechanism. In contrast to 4-OT, hh4-OT does not exhibit the low-level activity of another tautomerase superfamily member, the heterohexamer trans-3-chloroacrylic acid dehalogenase (CaaD). Characterization of hh4-OT enables functional assignment of the related enzymes, highlights the diverse ways the beta-alpha-beta building block can be assembled into an active enzyme, and provides further insight into the molecular basis of the low-level CaaD activity in 4-OT.
Kinetic and structural characterization of a heterohexamer 4-oxalocrotonate tautomerase from Chloroflexus aurantiacus J-10-fl: implications for functional and structural diversity in the tautomerase superfamily .,Burks EA, Fleming CD, Mesecar AD, Whitman CP, Pegan SD Biochemistry. 2010 Jun 22;49(24):5016-27. PMID:20465238[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Burks EA, Fleming CD, Mesecar AD, Whitman CP, Pegan SD. Kinetic and structural characterization of a heterohexamer 4-oxalocrotonate tautomerase from Chloroflexus aurantiacus J-10-fl: implications for functional and structural diversity in the tautomerase superfamily . Biochemistry. 2010 Jun 22;49(24):5016-27. PMID:20465238 doi:10.1021/bi100502z
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