|
|
(One intermediate revision by the same user not shown) |
Line 1: |
Line 1: |
|
| |
|
| ==Crystal Structure of DL-2-haloacid dehalogenase== | | ==Crystal Structure of DL-2-haloacid dehalogenase== |
| <StructureSection load='4n2x' size='340' side='right' caption='[[4n2x]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='4n2x' size='340' side='right'caption='[[4n2x]], [[Resolution|resolution]] 1.70Å' scene=''> |
| == Structural highlights == | | == 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> | | <table><tr><td colspan='2'>[[4n2x]] is a 6 chain structure with sequence from [https://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 [https://proteopedia.org/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> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4n2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n2x OCA], [https://pdbe.org/4n2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n2x RCSB], [https://www.ebi.ac.uk/pdbsum/4n2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n2x ProSAT]</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://pdbe.org/4n2x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n2x RCSB], [http://www.ebi.ac.uk/pdbsum/4n2x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n2x ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/A6BM74_9HYPH A6BM74_9HYPH] |
| 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>
| |
| <div class="pdbe-citations 4n2x" style="background-color:#fffaf0;"></div>
| |
|
| |
|
| ==See Also== | | ==See Also== |
| *[[Dehalogenase|Dehalogenase]] | | *[[Dehalogenase 3D structures|Dehalogenase 3D structures]] |
| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Methylobacterium sp. cpa1]] | | [[Category: Large Structures]] |
| [[Category: Esaki, N]] | | [[Category: Methylobacterium sp. CPA1]] |
| [[Category: Hirotsu, K]] | | [[Category: Esaki N]] |
| [[Category: Jitsumori, K]] | | [[Category: Hirotsu K]] |
| [[Category: Kurihara, T]] | | [[Category: Jitsumori K]] |
| [[Category: Omi, R]] | | [[Category: Kurihara T]] |
| [[Category: Paneth, P]] | | [[Category: Omi R]] |
| [[Category: Siwek, A]] | | [[Category: Paneth P]] |
| [[Category: Dehalogenase]]
| | [[Category: Siwek A]] |
| [[Category: Hydrolase]]
| |