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| <StructureSection load='4lbp' size='340' side='right'caption='[[4lbp]], [[Resolution|resolution]] 1.87Å' scene=''> | | <StructureSection load='4lbp' size='340' side='right'caption='[[4lbp]], [[Resolution|resolution]] 1.87Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4lbp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"pseudomonas_cepacia"_burkholder_1950 "pseudomonas cepacia" burkholder 1950]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LBP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LBP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4lbp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LBP FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1WG:2,5-DIHYDROXYCYCLOHEXA-2,5-DIENE-1,4-DIONE'>1WG</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]] 1.87Å</td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1WG:2,5-DIHYDROXYCYCLOHEXA-2,5-DIENE-1,4-DIONE'>1WG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lbh|4lbh]], [[4lbi|4lbi]]</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=4lbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lbp OCA], [https://pdbe.org/4lbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lbp RCSB], [https://www.ebi.ac.uk/pdbsum/4lbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lbp 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=4lbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lbp OCA], [http://pdbe.org/4lbp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lbp RCSB], [http://www.ebi.ac.uk/pdbsum/4lbp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lbp ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q45075_BURCE Q45075_BURCE] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Pseudomonas cepacia burkholder 1950]] | + | [[Category: Burkholderia cepacia]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Hayes, R P]] | + | [[Category: Hayes RP]] |
- | [[Category: Kang, C]] | + | [[Category: Kang C]] |
- | [[Category: Lewis, K M]] | + | [[Category: Lewis KM]] |
- | [[Category: Xun, L]] | + | [[Category: Xun L]] |
- | [[Category: Lyase]]
| + | |
| Structural highlights
Function
Q45075_BURCE
Publication Abstract from PubMed
TftG, 5-chloro-2-hydroxyhydroquinone (5-CHQ) dehydrochlorinase, is involved in the biodegradation of 2,4,5-trichlorophenoxyacetate by Burkholderia phenoliruptrix AC1100. It belongs to the YCII superfamily, a group of proteins with largely unknown function. In this work, we utilized structural and functional studies, including the apo-form and 2,5-dihydroxybenzoquinone binary complex crystal structures, computational analysis, and site-directed mutagenesis, to determine the dehydrochlorination mechanism. The His-Asp dyad, which initiates catalysis, is strongly conserved in YCII-like proteins. In addition, other catalytically important residues such as Pro-76, which orients the His-Asp catalytic dyad; Arg-17 and Ser-56, which form an oxyanion hole; and Asp-9, which stabilizes the oxyanion hole, are among the most highly conserved residues across the YCII superfamily members. The comprehensive characterization of TftG helps not only for identifying effective mechanisms for chloroaromatic dechlorination but also for understanding the functions of YCII superfamily members, which we propose to be lyases.
Catalytic Mechanism of 5-Chlorohydroxyhydroquinone Dehydrochlorinase from the YCII Superfamily of Largely Unknown Function.,Hayes RP, Lewis KM, Xun L, Kang C J Biol Chem. 2013 Oct 4;288(40):28447-28456. Epub 2013 Aug 16. PMID:23955343[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hayes RP, Lewis KM, Xun L, Kang C. Catalytic Mechanism of 5-Chlorohydroxyhydroquinone Dehydrochlorinase from the YCII Superfamily of Largely Unknown Function. J Biol Chem. 2013 Oct 4;288(40):28447-28456. Epub 2013 Aug 16. PMID:23955343 doi:http://dx.doi.org/10.1074/jbc.M113.499368
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