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==Crystal Structure of DL-2-haloacid dehalogenase== | |||
=== | <StructureSection load='4n2x' size='340' side='right' caption='[[4n2x]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4n2x]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Methylobacterium_sp._cpa1 Methylobacterium sp. cpa1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N2X FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dl-dex ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=439332 Methylobacterium sp. CPA1])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-haloacid_dehalogenase_(configuration-inverting) 2-haloacid dehalogenase (configuration-inverting)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.10 3.8.1.10] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4n2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n2x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n2x RCSB], [http://www.ebi.ac.uk/pdbsum/4n2x PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Several pathways of biotic dechlorination can be found in enzymes, each characterized by different chlorine isotopic fractionation, which can thus serve as a signature of a particular mechanism. Unlike other dehalogenases, DL-2-haloacid dehalogenase, DL-DEX, converts both enantiomers of the substrate. Chlorine isotope effects for this enzyme are larger than in the case of other dehalogenases. Recently, the 3D structure of this enzyme became available and enabled us to model these isotope effects and seek their origin. We show that the elevated values of the chlorine kinetic isotope effects originate in part in the processes of binding and migration within the enzyme active site that precede the dehalogenation step. | |||
Binding modes of DL-2-haloacid dehalogenase revealed by crystallography, modeling and isotope effects studies.,Siwek A, Omi R, Hirotsu K, Jitsumori K, Esaki N, Kurihara T, Paneth P Arch Biochem Biophys. 2013 Sep 23;540(1-2):26-32. doi: 10.1016/j.abb.2013.09.012. PMID:24071515<ref>PMID:24071515</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
[[Category: Esaki, N | |||
[[Category: Hirotsu, K | ==See Also== | ||
[[Category: Jitsumori, K | *[[Dehalogenase|Dehalogenase]] | ||
[[Category: Kurihara, T | == References == | ||
[[Category: Omi, R | <references/> | ||
[[Category: Paneth, P | __TOC__ | ||
[[Category: Siwek, A | </StructureSection> | ||
[[Category: Methylobacterium sp. cpa1]] | |||
[[Category: Esaki, N]] | |||
[[Category: Hirotsu, K]] | |||
[[Category: Jitsumori, K]] | |||
[[Category: Kurihara, T]] | |||
[[Category: Omi, R]] | |||
[[Category: Paneth, P]] | |||
[[Category: Siwek, A]] | |||
[[Category: Dehalogenase]] | [[Category: Dehalogenase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 12:33, 5 January 2015
Crystal Structure of DL-2-haloacid dehalogenaseCrystal Structure of DL-2-haloacid dehalogenase
Structural highlights
Publication Abstract from PubMedSeveral pathways of biotic dechlorination can be found in enzymes, each characterized by different chlorine isotopic fractionation, which can thus serve as a signature of a particular mechanism. Unlike other dehalogenases, DL-2-haloacid dehalogenase, DL-DEX, converts both enantiomers of the substrate. Chlorine isotope effects for this enzyme are larger than in the case of other dehalogenases. Recently, the 3D structure of this enzyme became available and enabled us to model these isotope effects and seek their origin. We show that the elevated values of the chlorine kinetic isotope effects originate in part in the processes of binding and migration within the enzyme active site that precede the dehalogenation step. Binding modes of DL-2-haloacid dehalogenase revealed by crystallography, modeling and isotope effects studies.,Siwek A, Omi R, Hirotsu K, Jitsumori K, Esaki N, Kurihara T, Paneth P Arch Biochem Biophys. 2013 Sep 23;540(1-2):26-32. doi: 10.1016/j.abb.2013.09.012. PMID:24071515[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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