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Acta Crystallogr F Struct Biol Commun. 2014 Mar;70(Pt 3):320-5. doi: 10.1107/S2053230X14001502. Epub 2014 Feb 19.

Purification, crystallization and preliminary crystallographic analysis of the catalytic core of cystathionine β-synthase from Saccharomyces cerevisiae.

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  • 1Structural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, Edificio 800, 48160 Derio, Bizkaia , Spain.
  • 2Department of Pediatrics, University of Colorado School of Medicine, Aurora, CO 80045, USA.


Cystathionine β-synthase (CBS; EC catalyzes the condensation of homocysteine and serine to form cystathionine, with the release of water. In humans, deficiency in CBS activity is the most common cause of hyperhomocysteinaemia and homocystinuria. More than 160 pathogenic mutations in the human CBS gene have been described to date. Here, the purification and preliminary crystallographic analysis of the catalytic core of CBS from Saccharomyces cerevisiae (ScCBS) is described which, in contrast to other eukaryotic CBSs, lacks the N-terminal haem-binding domain and is considered to be a useful model for investigation of the pyridoxal-5'-phosphate-mediated reactions of human CBS (hCBS). The purified protein yielded two different crystal forms belonging to space groups P41212 and P212121, with unit-cell parameters a = b = 72.390, c = 386.794 Å and a = 58.156, b = 89.988, c = 121.687 Å, respectively. Diffraction data were collected to 2.7 and 3.1 Å resolution, respectively, using synchrotron radiation. Preliminary analysis of the X-ray data suggests the presence of ScCBS homodimers in both types of crystals.


CBS domain; S-adenosylmethionine; cystathionine β-synthase; cysteine biosynthesis; homocysteine; pyridoxal-5′-phosphate; transsulfuration pathway

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