1s0y
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1s0y |SIZE=350|CAPTION= <scene name='initialview01'>1s0y</scene>, resolution 2.30Å | |PDB= 1s0y |SIZE=350|CAPTION= <scene name='initialview01'>1s0y</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MLA:MALONIC ACID'>MLA</scene> | + | |LIGAND= <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s0y OCA], [http://www.ebi.ac.uk/pdbsum/1s0y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s0y RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Poelarends, G J.]] | [[Category: Poelarends, G J.]] | ||
[[Category: Whitman, C P.]] | [[Category: Whitman, C P.]] | ||
| - | [[Category: MLA]] | ||
[[Category: covalent modification]] | [[Category: covalent modification]] | ||
[[Category: dehalogenase]] | [[Category: dehalogenase]] | ||
| Line 36: | Line 38: | ||
[[Category: tautomerase family]] | [[Category: tautomerase family]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:35:51 2008'' |
Revision as of 20:35, 30 March 2008
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| , resolution 2.30Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The structure of trans-3-chloroacrylic acid dehalogenase, covalently inactivated by the mechanism-based inhibitor 3-bromopropiolate at 2.3 Angstrom resolution
Overview
Isomer-specific 3-chloroacrylic acid dehalogenases function in the bacterial degradation of 1,3-dichloropropene, a compound used in agriculture to kill plant-parasitic nematodes. The crystal structure of the heterohexameric trans-3-chloroacrylic acid dehalogenase (CaaD) from Pseudomonas pavonaceae 170 inactivated by 3-bromopropiolate shows that Glu-52 in the alpha-subunit is positioned to function as the water-activating base for the addition of a hydroxyl group to C-3 of 3-chloroacrylate and 3-bromopropiolate, whereas the nearby Pro-1 in the beta-subunit is positioned to provide a proton to C-2. Two arginine residues, alphaArg-8 and alphaArg-11, interact with the C-1 carboxylate groups, thereby polarizing the alpha,beta-unsaturated acids. The reaction with 3-chloroacrylate results in the production of an unstable halohydrin, 3-chloro-3-hydroxypropanoate, which decomposes into the products malonate semialdehyde and HCl. In the inactivation mechanism, however, malonyl bromide is produced, which irreversibly alkylates the betaPro-1. CaaD is related to 4-oxalocrotonate tautomerase, with which it shares an N-terminal proline. However, in 4-oxalocrotonate tautomerase, Pro-1 functions as a base participating in proton transfer within a hydrophobic active site, whereas in CaaD, the acidic proline is stabilized in a hydrophilic active site. The altered active site environment of CaaD thus facilitates a previously unknown reaction in the tautomerase superfamily, the hydration of the alpha,beta-unsaturated bonds of trans-3-chloroacrylate and 3-bromopropiolate. The mechanism for these hydration reactions represents a novel catalytic strategy that results in carbon-halogen bond cleavage.
About this Structure
1S0Y is a Protein complex structure of sequences from Pseudomonas pavonaceae. Full crystallographic information is available from OCA.
Reference
The X-ray structure of trans-3-chloroacrylic acid dehalogenase reveals a novel hydration mechanism in the tautomerase superfamily., de Jong RM, Brugman W, Poelarends GJ, Whitman CP, Dijkstra BW, J Biol Chem. 2004 Mar 19;279(12):11546-52. Epub 2003 Dec 29. PMID:14701869
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