9azo: Difference between revisions
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==Crystal structure of CHMS Dehydrogenase PmdC from Comamonas testosteroni bound to cofactor NADP== | |||
<StructureSection load='9azo' size='340' side='right'caption='[[9azo]], [[Resolution|resolution]] 2.34Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9azo]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Comamonas_testosteroni_ATCC_11996 Comamonas testosteroni ATCC 11996]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9AZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9AZO FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.34Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=9azo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9azo OCA], [https://pdbe.org/9azo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9azo RCSB], [https://www.ebi.ac.uk/pdbsum/9azo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9azo ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q93PS4_COMTE Q93PS4_COMTE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pyrone-2,4-dicarboxylic acid (PDC) is a valuable polymer precursor that can be derived from the microbial degradation of lignin. The key enzyme in the microbial production of PDC is CHMS dehydrogenase, which acts on the substrate 4-carboxy-2-hydroxymuconate-6-semialdehyde (CHMS). We present the crystal structure of CHMS dehydrogenase (PmdC from Comamonas testosteroni) bound to the cofactor NADP, shedding light on its three-dimensional architecture, and revealing residues responsible for binding NADP. Using a combination of structural homology, molecular docking, and quantum chemistry calculations we have predicted the binding site of CHMS. Key histidine residues in a conserved sequence are identified as crucial for binding the hydroxyl group of CHMS and facilitating dehydrogenation with NADP. Mutating these histidine residues results in a loss of enzyme activity, leading to a proposed model for the enzyme's mechanism. These findings are expected to help guide efforts in protein and metabolic engineering to enhance PDC yields in biological routes to polymer feedstock synthesis. | |||
Characterization of lignin degrading enzyme PmdC, which catalyzes a key step in the synthesis of polymer precursor 2-pyrone-4,6-dicarboxylic acid (PDC).,Rodrigues AV, Moriarty NW, Kakumanu R, DeGiovanni A, Pereira JH, Gin JW, Chen Y, Baidoo EEK, Petzold CJ, Adams PD J Biol Chem. 2024 Aug 31:107736. doi: 10.1016/j.jbc.2024.107736. PMID:39222681<ref>PMID:39222681</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9azo" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Comamonas testosteroni ATCC 11996]] | |||
[[Category: Large Structures]] | |||
[[Category: Adams PD]] | |||
[[Category: Moriarty NW]] | |||
[[Category: Pereira JH]] | |||
[[Category: Rodrigues AV]] | |||
