2dhc: Difference between revisions
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==CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE DEHALOGENASE== | ==CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE DEHALOGENASE== | ||
<StructureSection load='2dhc' size='340' side='right' caption='[[2dhc]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2dhc' size='340' side='right'caption='[[2dhc]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2dhc]] 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=2DHC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DHC FirstGlance]. <br> | <table><tr><td colspan='2'>[[2dhc]] 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=2DHC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DHC FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dh/2dhc_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dh/2dhc_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2dhc" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2dhc" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Dehalogenase 3D structures|Dehalogenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Corynebacterium autotrophicum baumgarten et al. 1974]] | [[Category: Corynebacterium autotrophicum baumgarten et al. 1974]] | ||
[[Category: Haloalkane dehalogenase]] | [[Category: Haloalkane dehalogenase]] | ||
[[Category: Large Structures]] | |||
[[Category: Dijkstra, B W]] | [[Category: Dijkstra, B W]] | ||
[[Category: Verschueren, K H.G]] | [[Category: Verschueren, K H.G]] | ||
[[Category: Dehalogenase]] | [[Category: Dehalogenase]] | ||
Revision as of 22:43, 11 December 2019
CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE DEHALOGENASECRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE DEHALOGENASE
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 PubMedCrystal 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 AlsoReferences
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