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Crystal structure of the pyridoxal-5'-phosphate-dependent serine dehydratase from human liver

¹ National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China
² Laboratory of Structural Biology, Medical School, Tsinghua University, Beijing 100084, China

(RECEIVED October 15, 2004; FINAL REVISION November 13, 2004; ACCEPTED November 19, 2004)

L-serine dehydratase (SDH), a member of the -family of pyridoxal phosphate-dependent (PLP) enzymes, catalyzes the deamination of L-serine and L-threonine to yield pyruvate or 2-oxobutyrate. The crystal structure of L-serine dehydratase from human liver (hSDH) has been solved at 2.5 Å-resolution by molecular replacement. The structure is a homodimer and reveals a fold typical for -family PLP-dependent enzymes. Each monomer serves as an active unit and is subdivided into two distinct domains: a small domain and a PLP-binding domain that covalently anchors the cofactor. Both domains show the typical open / architecture of PLP enzymes. Comparison with the rSDH-(PLP-OMS) holo-enzyme reveals a large structural difference in active sites caused by the artifical O-methylserine. Furthermore, the activity of hSDH-PLP was assayed and it proved to show catalytic activity. That suggests that the structure of hSDH-PLP is the first structure of the active natural holo-SDH.

Keywords: serine dehydratase; pyridoxal phosphate-dependent (PLP) enzyme; human liver; deamination; crystal structure

Abbreviations: SDH, serine dehydratase • TDH, threonine dehydratase • PLP, pyridoxal 5'-phosphate • hSDH human serine dehydratase • rSDH, rat serine dehydratase • eTDH, threonine deaminase from E. coli • d-eTDH, biodegradative threonine dehydratase from E. coli • -TRPS, tryptophan synthase -subunit • OASS, O-acetylserine sulfhydrylase • CBS, cystathione -synthase • ACCD, 1-aminocyclopropane-1-carboxylate deaminase • aTS, threonine synthase from A. thaliana • yTS, yeast threonine synthase • OPHS, O-phosphohomoserine

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.041179105.

Reprint requests to: Zihe Rao, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China; e-mail: raozh{at}ibp.ac.cn; fax: +86-10-6486-7566.

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