3zo7: Difference between revisions
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==Crystal structure of ClcFE27A with substrate== | |||
<StructureSection load='3zo7' size='340' side='right'caption='[[3zo7]], [[Resolution|resolution]] 2.22Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zo7]] 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=3ZO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZO7 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]] 2.224Å</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=K6H:(2S)-2-CHLORANYL-2-[(2R)-5-OXIDANYLIDENE-2H-FURAN-2-YL]ETHANOIC+ACID'>K6H</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=3zo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zo7 OCA], [https://pdbe.org/3zo7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zo7 RCSB], [https://www.ebi.ac.uk/pdbsum/3zo7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zo7 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3zo7" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Dehalogenase 3D structures|Dehalogenase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rhodococcus opacus]] | [[Category: Rhodococcus opacus]] | ||
[[Category: Groening | [[Category: Groening JAD]] | ||
[[Category: Kaschabek | [[Category: Kaschabek SR]] | ||
[[Category: Roth | [[Category: Roth C]] | ||
[[Category: Schloemann | [[Category: Schloemann M]] | ||
[[Category: Straeter | [[Category: Straeter N]] | ||
Latest revision as of 13:41, 9 May 2024
Crystal structure of ClcFE27A with substrateCrystal structure of ClcFE27A with substrate
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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