2dhe
From Proteopedia
(New page: 200px<br /><applet load="2dhe" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dhe, resolution 2.13Å" /> '''CRYSTALLOGRAPHIC ANA...) |
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| - | [[Image:2dhe.jpg|left|200px]]<br /><applet load="2dhe" size=" | + | [[Image:2dhe.jpg|left|200px]]<br /><applet load="2dhe" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2dhe, resolution 2.13Å" /> | caption="2dhe, resolution 2.13Å" /> | ||
'''CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE DEHALOGENASE'''<br /> | '''CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE DEHALOGENASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Crystal structures of haloalkane dehalogenase were determined in the | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2DHE 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:// | + | 2DHE 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 <scene name='pdbligand=CL:'>CL</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2DHE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xanthobacter autotrophicus]] | [[Category: Xanthobacter autotrophicus]] | ||
| - | [[Category: Dijkstra, B | + | [[Category: Dijkstra, B W.]] |
| - | [[Category: Verschueren, K | + | [[Category: Verschueren, K H.G.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: dehalogenase]] | [[Category: dehalogenase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:58:49 2008'' |
Revision as of 14:58, 21 February 2008
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CRYSTALLOGRAPHIC ANALYSIS OF THE CATALYTIC MECHANISM OF HALOALKANE DEHALOGENASE
Overview
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.
About this Structure
2DHE is a Single protein structure of sequence from Xanthobacter autotrophicus with as ligand. Active as Haloalkane dehalogenase, with EC number 3.8.1.5 Full crystallographic information is available from OCA.
Reference
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
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