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==Crystal structure of 5-chloro-2-hydroxymuconate tautomerase CnbG==
<StructureSection load='7xuy' size='340' side='right'caption='[[7xuy]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7xuy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Comamonas_testosteroni_CNB-1 Comamonas testosteroni CNB-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XUY 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]] 2.001&#8491;</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=7xuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xuy OCA], [https://pdbe.org/7xuy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xuy RCSB], [https://www.ebi.ac.uk/pdbsum/7xuy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xuy ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The catechol meta-cleavage pathway is widely involved in the degradation of aromatic compounds, including those halogenated aromatic hydrocarbons and their derivatives. CnbG is a kind of 4-oxalocrotonate tautomerase (4-OT) located in the catechol meta-cleavage pathway, catalyzes the ketonization of cis,cis-5-chloro-2-hydroxymuconate and cis,cis-2-hydroxymuconate to yield 5-chloro-2-oxo-3-hexene-1,6-dioate and 2-oxo-3-hexene-1,6-dioate, and contributes to the degradation of 4-chloronitrobenzene and chlorobenzene in Comamonas testosteroni CNB-1. Yet, the reason why CnbG and those 4-OTs could recognize various substrates is not well explained. Here, we determined the crystal structure of CnbG at resolution of 2.0 A and identified that the potential substrate pocket involved in four conserved residues, residues Pro1, Arg11, Arg39 and Trp50, but not five conserved residues as those reported in other 4-OTs. We also found the four conserved residues assemble different sequence patterns in different 4-OTs, indicating their potential roles in catalysis and substrate binding. Via molecular docking, we found the 5-chloro group was clamped by two residues and extended to the solvent, indicating a substrate binding mode that could bear the substitution of different groups in the 5-position. Our work extends the knowledge of the substrate specificity of enzymes in the catechol meta-cleavage pathway.

Structural insights into the substrate specificity of 5-chloro-2-hydroxymuconate tautomerase CnbG.,Ma HL, Ding M, Guo L, Li DF Biochem Biophys Res Commun. 2022 Sep 10;620:42-48. doi: , 10.1016/j.bbrc.2022.06.058. Epub 2022 Jun 22. PMID:35777133<ref>PMID:35777133</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7xuy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Comamonas testosteroni CNB-1]]
[[Category: Large Structures]]
[[Category: Li DF]]
[[Category: Ma HL]]