View source for 3znu


==Crystal structure of ClcF in crystal form 2==
<StructureSection load='3znu' size='340' side='right'caption='[[3znu]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3znu]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_opacus Rhodococcus opacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZNU 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]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3znu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3znu OCA], [https://pdbe.org/3znu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3znu RCSB], [https://www.ebi.ac.uk/pdbsum/3znu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3znu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8G9L0_RHOOP Q8G9L0_RHOOP] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The actinobacterium Rhodococcus opacus 1CP possesses a so far unique variant of the modified 3-oxoadipate pathway for 3-chlorocatechol degradation. One important feature is the novel dehalogenase ClcF, which converts (4R,5S) 5-chloromuconolactone to E-dienelactone. ClcF is related to muconolactone isomerase (MLI, EC 5.3.3.4). The enzyme has a ferredoxin-type fold and forms a homodecamer of 52-symmetry, typical for the MLI family. The active site is formed by residues from two monomers. The complex structure of an E27A variant with bound substrate in conjunction with mutational studies indicate that E27 acts as the proton acceptor in a univalent single-base syn-dehydrohalogenation mechanism. Despite the evolutionary specialisation of ClcF, the conserved active site structures suggest that the proposed mechanism is representative for the MLI family. Furthermore, ClcF represents a novel type of dehalogenase based on an isomerase scaffold.

Crystal structure and catalytic mechanism of chloromuconolactone dehalogenase ClcF from Rhodococcus opacus 1CP.,Roth C, Janosch AD, Kaschabek SR, Schlomann M, Strater N Mol Microbiol. 2013 Feb 20. doi: 10.1111/mmi.12182. PMID:23421784<ref>PMID:23421784</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3znu" style="background-color:#fffaf0;"></div>

==See Also==
*[[Dehalogenase 3D structures|Dehalogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodococcus opacus]]
[[Category: Groening JAD]]
[[Category: Kaschabek SR]]
[[Category: Roth C]]
[[Category: Schloemann M]]
[[Category: Straeter N]]