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. 2013 Oct;69(Pt 10):1131-4.
doi: 10.1107/S1744309113023956. Epub 2013 Sep 28.

Crystallization and preliminary X-ray diffraction studies of D-threo-3-hydroxyaspartate dehydratase isolated from Delftia sp. HT23

Yu Matsumoto  1 , Yoshiaki Yasutake, Yuki Takeda, Tomohiro Tamura, Atsushi Yokota, Masaru Wada
Affiliations

Crystallization and preliminary X-ray diffraction studies of D-threo-3-hydroxyaspartate dehydratase isolated from Delftia sp. HT23

Yu Matsumoto et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Oct.

Abstract

D-threo-3-Hydroxyaspartate dehydratase (D-THA DH) isolated from the soil bacterium Delftia sp. HT23 is a novel enzyme consisting of 380 amino-acid residues which catalyzes the conversion of D-threo-3-hydroxyaspartate to oxaloacetate and ammonia. D-THA DH also catalyzes the dehydration of L-threo-3-hydroxyaspartate, L-erythro-3-hydroxyaspartate and D-serine. The amino-acid sequence of D-THA DH shows significant similarity to that of two eukaryotic D-serine dehydratases derived from Saccharomyces cerevisiae and chicken kidney. D-THA DH is classified into the fold-type III group of pyridoxal enzymes and is the first example of a fold-type III dehydratase derived from a prokaryote. Overexpression of recombinant D-THA DH was carried out using a Rhodococcus erythropolis expression system and the obtained protein was subsequently purified and crystallized. The crystals of D-THA DH belonged to space group I4₁22, with unit-cell parameters a=b=157.3, c=157.9 Å. Single-wavelength anomalous diffraction data were collected to a resolution of 2.0 Å using synchrotron radiation at the wavelength of the Br K absorption edge.

Keywords: Br-SAD; Delftia sp. HT23; alanine racemase; d-threo-3-hydroxyaspartate dehydratase; pyridoxal 5′-phosphate.

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Figures

Figure 1
Figure 1
Scheme of the reactions catalyzed by d-threo-3-hydroxyaspartate dehydratase (d-THA DH).
Figure 2
Figure 2
Typical crystals of d-threo-3-hydroxyaspartate dehydratase (d-THA DH). The crystal used for the current study was obtained with 0.1 M Tris pH 8.5, 0.2 M MgCl2, 13% PEG 3350.
Figure 3
Figure 3
An X-ray diffraction pattern obtained on the NW-12A beamline at PF, Japan from a single crystal of d-threo-3-hydroxyaspartate dehydratase (d-THA DH).
See this image and copyright information in PMC

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