1px0
From Proteopedia
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'''Crystal structure of the haloalcohol dehalogenase HheC complexed with the haloalcohol mimic (R)-1-para-nitro-phenyl-2-azido-ethanol''' | '''Crystal structure of the haloalcohol dehalogenase HheC complexed with the haloalcohol mimic (R)-1-para-nitro-phenyl-2-azido-ethanol''' | ||
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[[Category: Tang, L.]] | [[Category: Tang, L.]] | ||
[[Category: Tiesinga, J J.W.]] | [[Category: Tiesinga, J J.W.]] | ||
| - | [[Category: | + | [[Category: Haloalcohol dehalogenase]] |
| - | [[Category: | + | [[Category: Halohydrin dehalogenase]] |
| - | [[Category: | + | [[Category: Halohydrin hydrogen-halide lyase]] |
| - | [[Category: | + | [[Category: Rossmann fold]] |
| - | [[Category: | + | [[Category: Sdr family]] |
| - | [[Category: | + | [[Category: Short-chain dehydrogenase/reductase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:35:04 2008'' | |
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Revision as of 02:35, 3 May 2008
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 Page seeded by OCA on Sat May 3 05:35:04 2008
Categories: Agrobacterium tumefaciens | Single protein | Dijkstra, B W. | Janssen, D B. | Jong, R M.de. | Kalk, K H. | Rozeboom, H J. | Tang, L. | Tiesinga, J J.W. | Haloalcohol dehalogenase | Halohydrin dehalogenase | Halohydrin hydrogen-halide lyase | Rossmann fold | Sdr family | Short-chain dehydrogenase/reductase
