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

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 57; no. 2; pp. 289 - 291
• Main Authors: Janosik, Miroslav, Meier, Markus, Kery, Vladimir, Oliveriusova, Jana, Burkhard, Peter, Kraus, Jan P.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01.02.2001
• Subjects: Binding Sites; Cloning, Molecular; Crystallization; Cystathionine beta-Synthase - chemistry; Cystathionine beta-Synthase - isolation & purification; Cystathionine beta-Synthase - metabolism; cystathionine β-synthase; Escherichia coli; heme; homocysteine; homocystinuria; Humans; Recombinant Proteins - chemistry; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; Sequence Deletion; transsulfuration; Vascular Diseases - enzymology; X-Ray Diffraction
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444900017893

Cystathionine β‐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 Å which belong to space group P31 or P32. This is the first comprehensive structural investigation of a PLP and heme‐containing enzyme.