Crystallization and preliminary X-ray study of recombinant betaine-homocysteine S-methyltransferase from rat liver.
Betaine-homocysteine S-methyltransferase is one of the three enzymes involved in homocysteine catabolism. It uses betaine as the methyl donor to convert homocysteine into methionine, also producing dimethylglycine. Recombinant BHMT from rat liver was crystallized by the vapour-diffusion method in both native and seleniomethionyl-labelled forms. Crystals belong to space group P2(1), with unit-cell parameters a = 57.8, b = 149.3, c = 96.2 A, beta = 92.9 degrees. Data from native, seleniomethionine-labelled and two heavy-atom derivatives were collected using synchrotron sources. Self-rotation function and sedimentation-velocity experiments suggest that the enzyme is tetrameric with 222 symmetry.
Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto de Química-Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.
Beatriz
B
González
María A
MA
Pajares
Heng Phon
HP
Too
Francisco
F
Garrido
T L
TL
Blundell
Julia
J
Sanz-Aparicio
D000818:Animals; D001483:Base Sequence; D050940:Betaine-Homocysteine S-Methyltransferase; D003460:Crystallization; D018360:Crystallography, X-Ray; D017931:DNA Primers; D008099:Liver / Q000201:enzymology*; D008780:Methyltransferases / Q000737:chemistry*; D011487:Protein Conformation; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry
D017931:DNA Primers; D011994:Recombinant Proteins; D008780:Methyltransferases; D050940:Betaine-Homocysteine S-Methyltransferase; C494550:Bhmt protein, rat