Crystallization and preliminary X-ray diffraction analysis of the active core of human recombinant cystathionine beta-synthase: an enzyme involved in vascular disease.
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.
Janosik
M
M
Department of Pediatrics, University of Colorado School of Medicine, Denver, CO 80262, USA.
Meier
M
M
Kery
V
V
Oliveriusova
J
J
Burkhard
P
P
Kraus
J P
JP
D001665:Binding Sites; D003001:Cloning, Molecular; D003460:Crystallization; D003541:Cystathionine beta-Synthase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D004926:Escherichia coli; D006801:Humans; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D017384:Sequence Deletion; D014652:Vascular Diseases / Q000201:enzymology; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D003541:Cystathionine beta-Synthase