2dhc
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=DCE:1,2-DICHLOROETHANE'>DCE</scene> | |LIGAND= <scene name='pdbligand=DCE:1,2-DICHLOROETHANE'>DCE</scene> | ||
| - | |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] | + | |ACTIVITY= <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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dhc OCA], [http://www.ebi.ac.uk/pdbsum/2dhc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dhc RCSB]</span> | ||
}} | }} | ||
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[[Category: Dijkstra, B W.]] | [[Category: Dijkstra, B W.]] | ||
[[Category: Verschueren, K H.G.]] | [[Category: Verschueren, K H.G.]] | ||
| - | [[Category: DCE]] | ||
[[Category: dehalogenase]] | [[Category: dehalogenase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:34:43 2008'' |
Revision as of 23:34, 30 March 2008
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| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Haloalkane dehalogenase, with EC number 3.8.1.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
2DHC is a Single protein structure of sequence from Xanthobacter autotrophicus. 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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