EC Number   |
|---|
    2.1.1.13 | 3.0 A structure of a 65000 Da C-terminal fragment of methionine synthase that spans the cobalamin- and the S-adenosylmethionine-binding domains, arranged in a conformation suitable for the methyl transfer from S-adenosylmethionine to cobalamin that occurs during activation |
| 2.1.1.13 | cobalamin-binding domain |
| 2.1.1.13 | design and preparation of myoglobin reconstituted with the cobalt corrinoid complex, Co(TDHC) as a simple model for the active site. In the heme pocket of myoglobin, CoII(TDHC) is tightly bound and provides a model of the baseoff/His-on state of the cobalamin binding domain of methionine synthase, and the intermediate, the tetra-coordinated Co(I) species, is detectable in the protein matrix |
| 2.1.1.13 | docking studies for inhibitors 4-(7-nitroquinoxalin-2-yl)benzoic acid, N-[(5-nitro-1H-benzimidazol-2-yl)methyl]benzamide, and 4-nitro-N-[2-(5-nitro-1H-benzimidazol-2-yl)ethyl]benzamide. Polar residues within the binding site of 5-methyltetrahydrofolate, namely, Asn404, Asn458, Asp525, Asn567, and Arg579, are critical for the interaction with substrate |
| 2.1.1.13 | hanging drop vapor diffusion method using 0.2 M potassium nitrate, 18% (w/v) PEG3350, or microbatch vapor diffusion method using 0.2 M potassium nitrate, 20% (w/v) PEG3350, 50 mM HEPES pH 7.5 |
| 2.1.1.13 | hanging drop vapor diffusion method, using 25% 1,2-propanediol, 10% (v/v) glycerol, 5% (w/v) PEG 3000, 100 mM potassium citrate, pH 4.8, 15% (v/v) 1,2,3-heptanetriol, and 100 mM YCl3 (final pH, 5.2), at 4°C |
| 2.1.1.13 | hybrid quantum mechanics/molecular mechanics computations reveal the traditionally assumed SN2 mechanism for formation the CH3-cob(III)alamin resting state. The activation energy barrier for the SN2 reaction is 8-9 kcal/mol, which is comparable with respect to the determined experimental rate constant. Alternatively, an electron transfer based radical mechanism is possible, where first an electron transfer from His-on cob(I)alamin to the pterin ring of the protonated CH3-H4-folate takes place, forming the CoII(d7)-pterin radical diradical state, followed by a methyl radical transfer. The major advantage of electron transfer is that a methyl radical can be transferred at a longer distance, which does not require the close proximity of two binding modules of MetH as does the SN2 type. The protonation event must take place either prior to or during the methyl transfer reaction in a ternary complex |
| 2.1.1.13 | sitting drop vapour diffusion method in reservoir solution of 0.1 M Tris/HCl pH 7.5 containing 0.1-0.4 M sodium acetate, 10-12% poly(ethylene glycol) 8000 and 10-12% poly(ethyleneglycol) 1000 |
| 2.1.1.13 | sitting drop vapour diffusion method, crystal structures of the N-terminal substrate-binding module of the enzyme and their complexes with the substrates L-homocysteine and 5-methyltetrahydrofolate |
| 2.1.1.13 | the 65-kDa I690C/G743C MetH fragment is crystallized by the microbatch method, using 0.2 M potassium nitrate and 20% (w/v) PEG3350 |
