EC Number   |
|---|
   2.1.1.180 | apo-enzyme, to 1.8 A resolution, by molecular replacement. Kmr possesses a canonical S-adenosylmethionine binding pocket but with reduced sensitivity to mutation |
| 2.1.1.180 | electrostatic interactions made by the NpmA beta2/3 linker collectively are critical for docking of NpmA on a conserved 16S rRNA tertiary surface. Other NpmA regions (beta5/beta6 and beta6/beta7 linkers) contain several residues critical for optimal positioning of A1408 but are largely dispensable for 30S binding. In a model for NpmA action, 30S binding and adoption of a catalytically competent state are distinct: docking on 16S rRNA via the beta2/3 linker necessarily precedes functionally critical 30S substrate-driven conformational changes elsewhere in NpmA |
| 2.1.1.180 | H/D exchange mass spectrometry of apo NpmA in the presence and absence of SAM/SAH. Ligand binding results in time-dependent differences in deuterium exchange not only at the ligand-binding pocket (residues D25-D55 and A86-E112) but also in distal regions (F62-F82 and Y113-S144) of NpmA |
| 2.1.1.180 | hanging drop vapor diffusion method, using 0.03 M Bis-Tris (pH 5.5) and 25.5% (w/v) polyethylene glycol 3350 |
| 2.1.1.180 | high-resolution crystal structures of KamB from Streptoalloteichus tenebrarius is determined at 1.69 A |
| 2.1.1.180 | high-resolution crystal structures of NpmA from Escherichia coli is determined at 1.69 A |
| 2.1.1.180 | in complex with the 30S ribosome subunit and sinefungin |
