7kd9: Difference between revisions
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==Crystal Structure of Gallic Acid Decarboxylase from Arxula adeninivorans== | ==Crystal Structure of Gallic Acid Decarboxylase from Arxula adeninivorans== | ||
<StructureSection load='7kd9' size='340' side='right'caption='[[7kd9]]' scene=''> | <StructureSection load='7kd9' size='340' side='right'caption='[[7kd9]], [[Resolution|resolution]] 1.94Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KD9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7kd9]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Blastobotrys_adeninivorans Blastobotrys adeninivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KD9 FirstGlance]. <br> | ||
</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=7kd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kd9 OCA], [https://pdbe.org/7kd9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kd9 RCSB], [https://www.ebi.ac.uk/pdbsum/7kd9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kd9 ProSAT]</span></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]] 1.94Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</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=7kd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kd9 OCA], [https://pdbe.org/7kd9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kd9 RCSB], [https://www.ebi.ac.uk/pdbsum/7kd9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kd9 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A060TAG5_BLAAD A0A060TAG5_BLAAD] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Hydroxybenzoic acids, like gallic acid and protocatechuic acid, are highly abundant natural compounds. In biotechnology, they serve as critical precursors for various molecules in heterologous production pathways, but a major bottleneck is these acids' non-oxidative decarboxylation to hydroxybenzenes. Optimizing this step by pathway and enzyme engineering is tedious, partly because of the complicating cofactor dependencies of the commonly used prFMN-dependent decarboxylases. Here, we report the crystal structures (1.5-1.9 A) of two homologous fungal decarboxylases, AGDC1 from Arxula adenivorans, and PPP2 from Madurella mycetomatis. Remarkably, both decarboxylases are cofactor independent and are superior to prFMN-dependent decarboxylases when heterologously expressed in Saccharomyces cerevisiae. The organization of their active site, together with mutational studies, suggests a novel decarboxylation mechanism that combines acid-base catalysis and transition state stabilization. Both enzymes are trimers, with a central potassium binding site. In each monomer, potassium introduces a local twist in a beta-sheet close to the active site, which primes the critical H86-D40 dyad for catalysis. A conserved pair of tryptophans, W35 and W61, acts like a clamp that destabilizes the substrate by twisting its carboxyl group relative to the phenol moiety. These findings reveal AGDC1 and PPP2 as founding members of a so far overlooked group of cofactor independent decarboxylases and suggest strategies to engineer their unique chemistry for a wide variety of biotechnological applications. | |||
Crystal structures of non-oxidative decarboxylases reveal a new mechanism of action with a catalytic dyad and structural twists.,Zeug M, Markovic N, Iancu CV, Tripp J, Oreb M, Choe JY Sci Rep. 2021 Feb 4;11(1):3056. doi: 10.1038/s41598-021-82660-z. PMID:33542397<ref>PMID:33542397</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7kd9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Blastobotrys adeninivorans]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Choe J]] | [[Category: Choe J]] | ||
