Crystallization and preliminary X-ray diffraction analysis of the active core of human recombinant cystathionine beta-synthase: an enzyme involved in vascular disease.

Abstract

Cystathionine beta-synthase (CBS) is a unique heme enzyme that catalyzes a PLP-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an autosomal recessively inherited disease of sulfur metabolism. A truncated form of CBS in which the C-terminal amino-acid residues have been deleted has been prepared. The truncated CBS subunits form a dimer, in contrast to the full-length subunits which form tetramers and higher oligomers. The truncated CBS yielded crystals diffracting to 2.6 A which belong to space group P3(1) or P3(2). This is the first comprehensive structural investigation of a PLP and heme-containing enzyme.

• Authors: M Janosik, M Meier, V Kery, J Oliveriusova, P Burkhard, J P Kraus
• Journal: Acta crystallographica. Section D, Biological crystallography (Acta Crystallogr D Biol Crystallogr) Vol. 57 Issue Pt 2 Pg. 289-91 (Feb 2001) ISSN: 0907-4449 [Print] United States
• PMID: 11173483 (Publication Type: Journal Article)

Chemical References

• Recombinant Proteins
• Cystathionine beta-Synthase

Topics

• Binding Sites
• Cloning, Molecular
• Crystallization
• Cystathionine beta-Synthase (chemistry, isolation & purification, metabolism)
• Escherichia coli
• Humans
• Recombinant Proteins (chemistry, isolation & purification, metabolism)
• Sequence Deletion
• Vascular Diseases (enzymology)
• X-Ray Diffraction