9k2j: Difference between revisions
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==X-ray crystal structure of 3-hydroxyisobutyrate dehydrogenase== | |||
<StructureSection load='9k2j' size='340' side='right'caption='[[9k2j]], [[Resolution|resolution]] 2.88Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9k2j]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_sp. Desulfovibrio sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9K2J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9K2J 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]] 2.88Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=9k2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9k2j OCA], [https://pdbe.org/9k2j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9k2j RCSB], [https://www.ebi.ac.uk/pdbsum/9k2j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9k2j ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ubiquitous R- and S-enantiomers of 2,3-dihydroxypropanesulfonate (DHPS), organic sulfur compounds produced by photosynthetic organisms, serve as common nutrient and energy sources for specific bacteria. While most known DHPS-degrading enzymes exhibit enantioselectivity, this study introduces a unique dehydrogenase, DhpA from the sulfate-reducing bacterium Desulfovibrio sp. DF1, capable of efficiently metabolizing both R- and S-DHPS to 3-sulfolactaldehyde (SLA). The crystal structure of DhpA reveals a conserved binding pocket that recognizes the sulfonate group of DHPS through interactions with Lys123, Ser174, and Asn175. The catalytic mechanism of the enzyme involves the oxidation of the C3-OH group of both enantiomers, facilitated by the Lys171. The mutation of Lys171 significantly diminishes activity, confirming its critical role in catalysis. Based on biochemical and genetic analyses, this study proposes a chiral DHPS degradation pathway in bacteria. This study reveals the unique enantiomeric selectivity of DhpA, expanding our understanding of the bacterial metabolism of chiral molecules. | |||
Mirror substrates specificity of a 2, 3-dihydroxypropanesulfonate degrading enzyme in sulfate-reducing bacteria.,Ma X, Wang H, Liu L, Dang H, Tang K Int J Biol Macromol. 2025 Mar 5;306(Pt 4):141806. doi: , 10.1016/j.ijbiomac.2025.141806. PMID:40054810<ref>PMID:40054810</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Tang | <div class="pdbe-citations 9k2j" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Desulfovibrio sp]] | |||
[[Category: Large Structures]] | |||
[[Category: Tang K]] | |||
Latest revision as of 06:36, 19 March 2025
X-ray crystal structure of 3-hydroxyisobutyrate dehydrogenase
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