8r2x
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of hydroxyquinol-1,2-dioxygenase from Rhodococcus jostii RHA1 (RjTsdC)== | |
| + | <StructureSection load='8r2x' size='340' side='right'caption='[[8r2x]], [[Resolution|resolution]] 1.57Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8r2x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_jostii_RHA1 Rhodococcus jostii RHA1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8R2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8R2X 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]] 1.573Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</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=8r2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8r2x OCA], [https://pdbe.org/8r2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8r2x RCSB], [https://www.ebi.ac.uk/pdbsum/8r2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8r2x ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q0SFL8_RHOJR Q0SFL8_RHOJR] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | White-rot fungi (WRF) are the most efficient lignin-degrading organisms in nature. However, their capacity to use lignin-related aromatic compounds, such as 4-hydroxybenzoate, as carbon sources has only been described recently. Previously, the hydroxyquinol pathway was proposed for the bioconversion of these compounds in fungi, but gene- and structure-function relationships of the full enzymatic pathway remain uncharacterized in any single fungal species. Here, we characterize seven enzymes from two WRF, Trametes versicolor and Gelatoporia subvermispora, which constitute a four-enzyme cascade from 4-hydroxybenzoate to beta-ketoadipate via the hydroxyquinol pathway. Furthermore, we solve the crystal structure of four of these enzymes and identify mechanistic differences with the closest bacterial and fungal structural homologs. Overall, this research expands our understanding of aromatic catabolism by WRF and establishes an alternative strategy for the conversion of lignin-related compounds to the valuable molecule beta-ketoadipate, contributing to the development of biological processes for lignin valorization. | ||
| - | + | Biochemical and structural characterization of enzymes in the 4-hydroxybenzoate catabolic pathway of lignin-degrading white-rot fungi.,Kuatsjah E, Schwartz A, Zahn M, Tornesakis K, Kellermyer ZA, Ingraham MA, Woodworth SP, Ramirez KJ, Cox PA, Pickford AR, Salvachua D Cell Rep. 2024 Nov 25;43(12):115002. doi: 10.1016/j.celrep.2024.115002. PMID:39589922<ref>PMID:39589922</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8r2x" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rhodococcus jostii RHA1]] | ||
| + | [[Category: Kuatsjah E]] | ||
| + | [[Category: Salvachua D]] | ||
| + | [[Category: Zahn M]] | ||
Current revision
Crystal structure of hydroxyquinol-1,2-dioxygenase from Rhodococcus jostii RHA1 (RjTsdC)
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