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| | <StructureSection load='2dhd' size='340' side='right'caption='[[2dhd]], [[Resolution|resolution]] 2.13Å' scene=''> | | <StructureSection load='2dhd' size='340' side='right'caption='[[2dhd]], [[Resolution|resolution]] 2.13Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2dhd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"corynebacterium_autotrophicum"_baumgarten_et_al._1974 "corynebacterium autotrophicum" baumgarten et al. 1974]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DHD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2dhd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DHD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.13Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0AK:(2S)-2-AMINO-4-(2-CHLOROETHOXY)-4-OXOBUTANOIC+ACID'>0AK</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0AK:(2S)-2-AMINO-4-(2-CHLOROETHOXY)-4-OXOBUTANOIC+ACID'>0AK</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Haloalkane_dehalogenase Haloalkane dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.5 3.8.1.5] </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=2dhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dhd OCA], [https://pdbe.org/2dhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dhd RCSB], [https://www.ebi.ac.uk/pdbsum/2dhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dhd 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=2dhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dhd OCA], [http://pdbe.org/2dhd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dhd RCSB], [http://www.ebi.ac.uk/pdbsum/2dhd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dhd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DHLA_XANAU DHLA_XANAU]] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Has a broad substrate specificity, which includes terminally mono- and di- chlorinated and brominated alkanes (up to C4 only). The highest activity was found with 1,2-dichloroethane, 1,3-dichloropropane, and 1,2-dibromoethane. | + | [https://www.uniprot.org/uniprot/DHLA_XANAU DHLA_XANAU] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Has a broad substrate specificity, which includes terminally mono- and di- chlorinated and brominated alkanes (up to C4 only). The highest activity was found with 1,2-dichloroethane, 1,3-dichloropropane, and 1,2-dibromoethane. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Corynebacterium autotrophicum baumgarten et al. 1974]] | |
| - | [[Category: Haloalkane dehalogenase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dijkstra, B W]] | + | [[Category: Xanthobacter autotrophicus]] |
| - | [[Category: Verschueren, K H.G]] | + | [[Category: Dijkstra BW]] |
| - | [[Category: Dehalogenase]] | + | [[Category: Verschueren KHG]] |
| Structural highlights
Function
DHLA_XANAU Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Has a broad substrate specificity, which includes terminally mono- and di- chlorinated and brominated alkanes (up to C4 only). The highest activity was found with 1,2-dichloroethane, 1,3-dichloropropane, and 1,2-dibromoethane.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Crystal structures of haloalkane dehalogenase were determined in the presence of the substrate 1,2-dichloroethane. At pH 5 and 4 degrees C, substrate is bound in the active site without being converted; warming to room temperature causes the substrate's carbon-chlorine bond to be broken, producing a chloride ion with concomitant alkylation of the active-site residue Asp124. At pH 6 and room temperature the alkylated enzyme is hydrolysed by a water molecule activated by the His289-Asp260 pair in the active site. These results show that catalysis by the dehalogenase proceeds by a two-step mechanism involving an ester intermediate covalently bound at Asp124.
Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase.,Verschueren KH, Seljee F, Rozeboom HJ, Kalk KH, Dijkstra BW Nature. 1993 Jun 24;363(6431):693-8. PMID:8515812[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Verschueren KH, Seljee F, Rozeboom HJ, Kalk KH, Dijkstra BW. Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase. Nature. 1993 Jun 24;363(6431):693-8. PMID:8515812 doi:http://dx.doi.org/10.1038/363693a0
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