2dhc

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[[Image:2dhc.jpg|left|200px]]
 
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{{Structure
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==CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE DEHALOGENASE==
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|PDB= 2dhc |SIZE=350|CAPTION= <scene name='initialview01'>2dhc</scene>, resolution 2.3&Aring;
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<StructureSection load='2dhc' size='340' side='right'caption='[[2dhc]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=DCE:1,2-DICHLOROETHANE'>DCE</scene>
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<table><tr><td colspan='2'>[[2dhc]] 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=2DHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DHC FirstGlance]. <br>
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|ACTIVITY= [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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCE:1,2-DICHLOROETHANE'>DCE</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dhc OCA], [https://pdbe.org/2dhc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dhc RCSB], [https://www.ebi.ac.uk/pdbsum/2dhc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dhc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dh/2dhc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dhc ConSurf].
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<div style="clear:both"></div>
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'''CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE DEHALOGENASE'''
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==See Also==
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*[[Dehalogenase 3D structures|Dehalogenase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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==About this Structure==
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2DHC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DHC OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8515812 8515812]
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[[Category: Haloalkane dehalogenase]]
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[[Category: Single protein]]
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[[Category: Xanthobacter autotrophicus]]
[[Category: Xanthobacter autotrophicus]]
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[[Category: Dijkstra, B W.]]
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[[Category: Dijkstra BW]]
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[[Category: Verschueren, K H.G.]]
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[[Category: Verschueren KHG]]
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[[Category: DCE]]
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[[Category: dehalogenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:27:15 2008''
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Current revision

CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE DEHALOGENASE

PDB ID 2dhc

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