1edd

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(New page: 200px<br /><applet load="1edd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1edd, resolution 2.19&Aring;" /> '''CRYSTALLOGRAPHIC AND...)
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[[Image:1edd.jpg|left|200px]]<br /><applet load="1edd" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1edd, resolution 2.19&Aring;" />
 
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'''CRYSTALLOGRAPHIC AND FLUORESCENCE STUDIES OF THE INTERACTION OF HALOALKANE DEHALOGENASE WITH HALIDE IONS: STUDIES WITH HALIDE COMPOUNDS REVEAL A HALIDE BINDING SITE IN THE ACTIVE SITE'''<br />
 
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==Overview==
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==CRYSTALLOGRAPHIC AND FLUORESCENCE STUDIES OF THE INTERACTION OF HALOALKANE DEHALOGENASE WITH HALIDE IONS: STUDIES WITH HALIDE COMPOUNDS REVEAL A HALIDE BINDING SITE IN THE ACTIVE SITE==
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Haloalkane dehalogenase from Xanthobacter autotrophicus GJ10 catalyzes the, conversion of 1,2-dichloroethane to 2-chloroethanol and chloride without, use of oxygen or cofactors. The active site is situated in an internal, cavity, which is accessible from the solvent, even in the crystal. Crystal, structures of the dehalogenase enzyme complexed with iodoacetamide, chloroacetamide, iodide, and chloride at pH 6.2 and 8.2 revealed a halide, binding site between the ring NH's of two tryptophan residues, Trp-125 and, Trp-175, located in the active site. The halide ion lies on the, intersection of the planes of the rings of the tryptophans. The binding of, iodide and chloride to haloalkane dehalogenase caused a strong decrease in, protein fluorescence. The decrease could be fitted to a modified form of, the Stern-Volmer equation, indicating the presence of fluorophors of, different accessibilities. Halide binding was much stronger at pH 6.0 than, at pH 8.2. Assuming ligand binding to Trp-125 and Trp-175 as the sole, cause of fluorescence quenching, dissociation constants at pH 6.0 with, chloride and iodide were calculated to be 0.49 +/- 0.04 and 0.074 +/-, 0.007 mM, respectively. Detailed structural investigation showed that the, halide binding site probably stabilizes the halide product as well as the, negatively charged transition state occurring during the formation of the, covalent intermediate.
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<StructureSection load='1edd' size='340' side='right'caption='[[1edd]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1edd]] 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=1EDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EDD FirstGlance]. <br>
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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]] 2.19&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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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=1edd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edd OCA], [https://pdbe.org/1edd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1edd RCSB], [https://www.ebi.ac.uk/pdbsum/1edd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1edd 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/ed/1edd_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=1edd ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1EDD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EDD OCA].
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*[[Dehalogenase 3D structures|Dehalogenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions. Studies with halide compounds reveal a halide binding site in the active site., Verschueren KH, Kingma J, Rozeboom HJ, Kalk KH, Janssen DB, Dijkstra BW, Biochemistry. 1993 Sep 7;32(35):9031-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8369276 8369276]
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[[Category: Large Structures]]
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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: CL]]
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[[Category: dehalogenase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:54:57 2007''
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Current revision

CRYSTALLOGRAPHIC AND FLUORESCENCE STUDIES OF THE INTERACTION OF HALOALKANE DEHALOGENASE WITH HALIDE IONS: STUDIES WITH HALIDE COMPOUNDS REVEAL A HALIDE BINDING SITE IN THE ACTIVE SITE

PDB ID 1edd

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