1pwz
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1pwz |SIZE=350|CAPTION= <scene name='initialview01'>1pwz</scene>, resolution 2.50Å | |PDB= 1pwz |SIZE=350|CAPTION= <scene name='initialview01'>1pwz</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=RSO:R-STYRENE+OXIDE'>RSO</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1pwx|1PWX]], [[1px0|1PX0]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pwz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pwz OCA], [http://www.ebi.ac.uk/pdbsum/1pwz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pwz RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Tang, L.]] | [[Category: Tang, L.]] | ||
[[Category: Tiesinga, J J.W.]] | [[Category: Tiesinga, J J.W.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: RSO]] | ||
[[Category: haloalcohol dehalogenase]] | [[Category: haloalcohol dehalogenase]] | ||
[[Category: halohydrin dehalogenase]] | [[Category: halohydrin dehalogenase]] | ||
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[[Category: short-chain dehydrogenase/reductase]] | [[Category: short-chain dehydrogenase/reductase]] | ||
| - | ''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 23:05:41 2008'' |
Revision as of 20:05, 30 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1PWX, 1PX0
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the haloalcohol dehalogenase HheC complexed with (R)-styrene oxide and chloride
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
1PWZ 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 Sun Mar 30 23:05:41 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
