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EC Number
Crystallization (Commentary)
6.5 mg/ml purified native or selenomethionine-labeled, or Hg-labeled enzyme in complex with S-adenosyl-L-methionine, S-adenosyl-L-homocysteine, or the cap guanylate plus S-adenosyl-L-homocysteine, in 20 mM Tris-HCl, pH 8.0, 220 mM NaCl, vapour diffusion against a well solution of 1.2 M sodium potassium tartrate, 50 mM bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane, pH 6.0-6.2, and 20 mM DTT, X-ray diffraction structure determination and analysis at 2.0-2.7 A resolution, modeling
Ecm1-aza-S-adenosyl-L-methionine binary complex, by vapor diffusion, reveals that the inhibitor occupies the same site as S-adenosyl-L-methionine
Ecm1-sinefungin binary complex, by vapor diffusion, to 2.6 A resolution
structure-function relationships of the N7-MTase. The ExoN domain is closely involved in the activity of the N7-MTase. Two of the 12 critical residues essential for the N7-MTase are located at the N terminus of the core ExoN domain, reinforcing a role of the ExoN domain in the N7-MTase activity of nsp14. The other 10 critical residues are distributed throughout the N7-MTase domain but localized mainly in the S-adenosyl-L-methionine-binding pocket
Results 1 - 4 of 4