Crystallization and preliminary crystallographic analysis of the recombinant N-terminal domain of riboflavin synthase.
Riboflavin synthase catalyzes the final step in the biosynthesis of riboflavin. Animals and humans lack this enzyme, whereas many bacteria and certain yeasts are absolutely dependent on endogenous riboflavin synthesis. Riboflavin synthase is therefore an attractive target for chemotherapy. The N-terminal domain of riboflavin synthase forms a dimer in solution and is capable of strongly binding riboflavin. It can serve as a model for the binding site of the native enzyme. Structural information obtained from this domain at high resolution will be helpful in the determination of the binding mode of riboflavin and thus for the development of antimicrobial drugs. Here, the crystallization and preliminary crystallographic analysis of the N-terminal domain of riboflavin synthase are reported. The crystals belong to the space group C222(1), with unit-cell parameters a = 50.3, b = 104.7, c = 85.3 A, alpha = beta = gamma = 90 degrees, and diffract to 2.6 A resolution.
Meining
W
W
Södertörns Högskola, S-14104 Huddinge, Sweden, and Karolinska Institutet, Novum, Center for Structural Biochemistry, S-14157 Huddinge, Sweden. winfried.meining@csb.ki.se
Eberhardt
S
S
Bacher
A
A
Ladenstein
R
R
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D012258:Riboflavin Synthase / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D011994:Recombinant Proteins; D012258:Riboflavin Synthase