5cgz
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5cgz]] is a 2 chain structure with sequence from [https://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=5CGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CGZ FirstGlance]. <br> | <table><tr><td colspan='2'>[[5cgz]] is a 2 chain structure with sequence from [https://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=5CGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CGZ FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.103Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5cgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cgz OCA], [https://pdbe.org/5cgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cgz RCSB], [https://www.ebi.ac.uk/pdbsum/5cgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cgz 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=5cgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cgz OCA], [https://pdbe.org/5cgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cgz RCSB], [https://www.ebi.ac.uk/pdbsum/5cgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cgz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/GALB_PSEPK GALB_PSEPK] Catalyzes the conversion of oxalomesaconic acid enol (OMAenol) to 4-carboxy-4-hydroxy-2-oxoadipic acid (CHA). Mediates the third step of gallate degradation pathway.<ref>PMID:21219457</ref> | [https://www.uniprot.org/uniprot/GALB_PSEPK GALB_PSEPK] Catalyzes the conversion of oxalomesaconic acid enol (OMAenol) to 4-carboxy-4-hydroxy-2-oxoadipic acid (CHA). Mediates the third step of gallate degradation pathway.<ref>PMID:21219457</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Bacterial catabolism of lignin and its breakdown products is of interest for applications in industrial processing of ligno-biomass. The gallate degradation pathway of Pseudomonas putida KT2440 requires a 4-carboxy-2-hydroxymuconate (CHM) hydratase (GalB) which has 12% sequence identity to a previously identified CHM hydratase (LigJ) from Sphingomonas sp. SYK-6. The structure of GalB was determined and found to be a member of the PIG-L N-acetyl glucosamine deacetylase family, and is structurally distinct from the amidohydrolase fold of LigJ. LigJ has the same stereo-specificity as GalB, providing an example of convergent evolution for catalytic conversion of a common metabolite in bacterial aromatic degradation pathways. Purified GalB contained bound Zn2+ cofactor; however the enzyme is capable using Fe2+ and Co2+ with similar efficiencies. The general base aspartate in the PIG-L deacetylases is an alanine in GalB; replacement of the alanine with aspartate decreased the GalB catalytic efficiency for CHM by 9.5 x 104 fold and the variant enzyme did not have any detectable hydrolase activity. Kinetic analyses and pH dependency studies of the wild-type and variant enzymes suggests roles for the Glu48 and His164 in the catalytic mechanism. Comparison to the PIG-L deacetylases has led to a proposed mechanism for GalB wherein Glu48 positions and activates the metal ligated water for the hydration reaction and His164 acts as a catalytic acid. | ||
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| - | Structural and Kinetic Characterization of the 4-Carboxy-2-Hydroxymuconate Hydratase from the Gallate and Protocatechuate 4,5-Cleavage Pathways of Pseudomonas putida KT2440.,Mazurkewich S, Brott AS, Kimber MS, Seah SY J Biol Chem. 2016 Feb 11. pii: jbc.M115.682054. PMID:26867578<ref>PMID:26867578</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 5cgz" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of GalB, the 4-carboxy-2-hydroxymuconate hydratase, from Pseuodomonas putida KT2440
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