Preparation, crystallization and preliminary X-ray analysis of the methionine synthase (MetE) from Streptococcus mutans.
The Streptococcus mutans metE gene encodes methionine synthase (MetE), which catalyzes the direct transfer of a methyl group from methyltetrahydrofolate to homocysteine in the last step of methionine synthesis. metE was cloned into pET28a and the gene product was expressed at high levels in the Escherichia coli strain BL21 (DE3). MetE was purified to homogeneity using Ni(2+)-chelating chromatography followed by size-exclusion chromatography. Crystals of the protein were obtained by the hanging-drop vapour-diffusion method and diffracted to 2.2 A resolution. The crystal belongs to space group P2(1), with unit-cell parameters a = 52.85, b = 99.48, c = 77.88 A, beta = 94.55 degrees .
Fu
Tian Min
TM
National Laboratory of Protein Engineering and Plant Genetic Engineering, Peking University, Beijing 100871, People's Republic of China.
Zhang
Xiao Yan
XY
Li
Lan Fen
LF
Liang
Yu He
YH
Su
Xiao Dong
XD
D013766:5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase / Q000737:chemistry* / Q000302:isolation & purification; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D013295:Streptococcus mutans / Q000201:enzymology*
D001426:Bacterial Proteins; D013766:5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase