1px0

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[[Image:1px0.jpg|left|200px]]<br /><applet load="1px0" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1px0.jpg|left|200px]]
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caption="1px0, resolution 1.90&Aring;" />
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'''Crystal structure of the haloalcohol dehalogenase HheC complexed with the haloalcohol mimic (R)-1-para-nitro-phenyl-2-azido-ethanol'''<br />
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{{Structure
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|PDB= 1px0 |SIZE=350|CAPTION= <scene name='initialview01'>1px0</scene>, resolution 1.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=RPN:(R)-1-PARA-NITRO-PHENYL-2-AZIDO-ETHANOL'>RPN</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Crystal structure of the haloalcohol dehalogenase HheC complexed with the haloalcohol mimic (R)-1-para-nitro-phenyl-2-azido-ethanol'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1PX0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens] with <scene name='pdbligand=RPN:'>RPN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PX0 OCA].
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1PX0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PX0 OCA].
==Reference==
==Reference==
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Structure and mechanism of a bacterial haloalcohol dehalogenase: a new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site., de Jong RM, Tiesinga JJ, Rozeboom HJ, Kalk KH, Tang L, Janssen DB, Dijkstra BW, EMBO J. 2003 Oct 1;22(19):4933-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14517233 14517233]
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Structure and mechanism of a bacterial haloalcohol dehalogenase: a new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site., de Jong RM, Tiesinga JJ, Rozeboom HJ, Kalk KH, Tang L, Janssen DB, Dijkstra BW, EMBO J. 2003 Oct 1;22(19):4933-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14517233 14517233]
[[Category: Agrobacterium tumefaciens]]
[[Category: Agrobacterium tumefaciens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: short-chain dehydrogenase/reductase]]
[[Category: short-chain dehydrogenase/reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:33:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:30:01 2008''

Revision as of 11:30, 20 March 2008

Image:1px0.jpg


PDB ID 1px0

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the haloalcohol dehalogenase HheC complexed with the haloalcohol mimic (R)-1-para-nitro-phenyl-2-azido-ethanol


Overview

Haloalcohol dehalogenases are bacterial enzymes that catalyze the cofactor-independent dehalogenation of vicinal haloalcohols such as the genotoxic environmental pollutant 1,3-dichloro-2-propanol, thereby producing an epoxide, a chloride ion and a proton. Here we present X-ray structures of the haloalcohol dehalogenase HheC from Agrobacterium radiobacter AD1, and complexes of the enzyme with an epoxide product and chloride ion, and with a bound haloalcohol substrate mimic. These structures support a catalytic mechanism in which Tyr145 of a Ser-Tyr-Arg catalytic triad deprotonates the haloalcohol hydroxyl function to generate an intramolecular nucleophile that substitutes the vicinal halogen. Haloalcohol dehalogenases are related to the widespread family of NAD(P)H-dependent short-chain dehydrogenases/reductases (SDR family), which use a similar Ser-Tyr-Lys/Arg catalytic triad to catalyze reductive or oxidative conversions of various secondary alcohols and ketones. Our results reveal the first structural details of an SDR-related enzyme that catalyzes a substitutive dehalogenation reaction rather than a redox reaction, in which a halide-binding site is found at the location of the NAD(P)H binding site. Structure-based sequence analysis reveals that the various haloalcohol dehalogenases have likely originated from at least two different NAD-binding SDR precursors.

About this Structure

1PX0 is a Single protein structure of sequence from Agrobacterium tumefaciens. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of a bacterial haloalcohol dehalogenase: a new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site., de Jong RM, Tiesinga JJ, Rozeboom HJ, Kalk KH, Tang L, Janssen DB, Dijkstra BW, EMBO J. 2003 Oct 1;22(19):4933-44. PMID:14517233

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