1x42: Difference between revisions

Revision as of 05:12, 28 July 2008

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File:1x42.png

Template:STRUCTURE 1x42

Crystal structure of a haloacid dehalogenase family protein (PH0459) from Pyrococcus horikoshii OT3Crystal structure of a haloacid dehalogenase family protein (PH0459) from Pyrococcus horikoshii OT3

Template:ABSTRACT PUBMED 16385007

About this StructureAbout this Structure

1X42 is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the probable haloacid dehalogenase PH0459 from Pyrococcus horikoshii OT3., Arai R, Kukimoto-Niino M, Kuroishi C, Bessho Y, Shirouzu M, Yokoyama S, Protein Sci. 2006 Feb;15(2):373-7. Epub 2005 Dec 29. PMID:16385007

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OCA

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-'''Crystal structure of a haloacid dehalogenase family protein (PH0459) from Pyrococcus horikoshii OT3'''
+===Crystal structure of a haloacid dehalogenase family protein (PH0459) from Pyrococcus horikoshii OT3===
-==Overview==
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-PH0459, from the hyperthermophilic archaeon Pyrococcus horikoshii OT3, is a probable haloacid dehalogenase with a molecular mass of 26,725 Da. Here, we report the 2.0 A crystal structure of PH0459 (PDB ID: 1X42) determined by the multiwavelength anomalous dispersion method. The core domain has an alpha/beta structure formed by a six-stranded parallel beta-sheet flanked by six alpha-helices and three 3(10)-helices. One disulfide bond, Cys186-Cys212, forms a bridge between an alpha-helix and a 3(10)-helix, although PH0459 seems to be an intracellular protein. The subdomain inserted into the core domain has a four-helix bundle structure. The crystal packing suggests that PH0459 exists as a monomer. A structural homology search revealed that PH0459 resembles the l-2-haloacid dehalogenases l-DEX YL from Pseudomonas sp. YL and DhlB from Xanthobacter autotrophicus GJ10. A comparison of the active sites suggested that PH0459 probably has haloacid dehalogenase activity, but its substrate specificity may be different. In addition, the disulfide bond in PH0459 probably facilitates the structural stabilization of the neighboring region in the monomeric form, although the corresponding regions in l-DEX YL and DhlB may be stabilized by dimerization. Since heat-stable dehalogenases can be used for the detoxification of halogenated aliphatic compounds, PH0459 will be a useful target for biotechnological research.
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