Crystallization and preliminary X-ray crystallographic studies of recombinant human betaine-homocysteine S-methyltransferase.
Betaine-homocysteine S-methyltransferase (BHMT) catalyzes a reaction essential for regulation of methionine and homocysteine metabolism and the catabolism of choline in mammalian tissues. Human recombinant BHMT (MW = 45 kDa) has been crystallized by the hanging-drop vapor-diffusion method at 294 K using ethylene glycol as the precipitant. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 109.190, b = 91.319, c = 88.661 A, beta = 122.044 degrees, and diffract to 2.9 A resolution on a local rotating-anode X-ray source. Rotation-function analysis and the Matthews coefficient, V(M) = 2.46 A(3) Da(-1), are consistent with a dimer in the asymmetric unit, suggesting that the active enzyme is a tetramer with 222 symmetry.
Department of Pharmaceutical and Biomedical Sciences, Wilson College of Pharmacy, University of Georgia, Athens 30602, USA.
Bose N
Momany C
D050940:Betaine-Homocysteine S-Methyltransferase; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D008780:Methyltransferases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D011994:Recombinant Proteins; D008780:Methyltransferases; C494548:BHMT protein, human; D050940:Betaine-Homocysteine S-Methyltransferase