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2flz

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[[Image:2flz.gif|left|200px]]
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{{STRUCTURE_2flz| PDB=2flz | SCENE= }}
{{STRUCTURE_2flz| PDB=2flz | SCENE= }}
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'''The X-ray structure of cis-3-chloroacrylic acid dehalogenase (cis-CaaD) with a sulfate ion bound in the active site'''
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===The X-ray structure of cis-3-chloroacrylic acid dehalogenase (cis-CaaD) with a sulfate ion bound in the active site===
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==Overview==
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The bacterial degradation pathways for the nematocide 1,3-dichloropropene rely on hydrolytic dehalogenation reactions catalyzed by cis- and trans-3-chloroacrylic acid dehalogenases (cis-CaaD and CaaD, respectively). X-ray crystal structures of native cis-CaaD and cis-CaaD inactivated by (R)-oxirane-2-carboxylate were elucidated. They locate four known catalytic residues (Pro-1, Arg-70, Arg-73, and Glu-114) and two previously unknown, potential catalytic residues (His-28 and Tyr-103'). The Y103F and H28A mutants of these latter two residues displayed reductions in cis-CaaD activity confirming their importance in catalysis. The structure of the inactivated enzyme shows covalent modification of the Pro-1 nitrogen atom by (R)-2-hydroxypropanoate at the C3 position. The interactions in the complex implicate Arg-70 or a water molecule bound to Arg-70 as the proton donor for the epoxide ring-opening reaction and Arg-73 and His-28 as primary binding contacts for the carboxylate group. This proposed binding mode places the (R)-enantiomer, but not the (S)-enantiomer, in position to covalently modify Pro-1. The absence of His-28 (or an equivalent) in CaaD could account for the fact that CaaD is not inactivated by either enantiomer. The cis-CaaD structures support a mechanism in which Glu-114 and Tyr-103' activate a water molecule for addition to C3 of the substrate and His-28, Arg-70, and Arg-73 interact with the C1 carboxylate group to assist in substrate binding and polarization. Pro-1 provides a proton at C2. The involvement of His-28 and Tyr-103' distinguishes the cis-CaaD mechanism from the otherwise parallel CaaD mechanism. The two mechanisms probably evolved independently as the result of an early gene duplication of a common ancestor.
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(as it appears on PubMed at http://www.pubmed.gov), where 17121835 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17121835}}
==About this Structure==
==About this Structure==
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[[Category: Dehalogenation]]
[[Category: Dehalogenation]]
[[Category: Hydratase]]
[[Category: Hydratase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:03:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:08:31 2008''

Revision as of 12:08, 27 July 2008

Image:2flz.png

Template:STRUCTURE 2flz

The X-ray structure of cis-3-chloroacrylic acid dehalogenase (cis-CaaD) with a sulfate ion bound in the active site

Template:ABSTRACT PUBMED 17121835

About this Structure

2FLZ is a Single protein structure of sequence from Coryneform bacterium. Full crystallographic information is available from OCA.

Reference

Crystal structures of native and inactivated cis-3-chloroacrylic acid dehalogenase. Structural basis for substrate specificity and inactivation by (R)-oxirane-2-carboxylate., de Jong RM, Bazzacco P, Poelarends GJ, Johnson WH Jr, Kim YJ, Burks EA, Serrano H, Thunnissen AM, Whitman CP, Dijkstra BW, J Biol Chem. 2007 Jan 26;282(4):2440-9. Epub 2006 Nov 22. PMID:17121835

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