EC Number   |
|---|
   2.3.1.82 | crystallized with its cofactor coenzyme A in space group C222(1), with unit cell parameters a = 71.5, b = 127.4, c = 76.9 A and one physiologically relevant dimer species per asymmetric unit |
| 2.3.1.82 | hanging drop vapor diffusion technique, crystal structure of the 6'-N-acetyltransferase type li in complex with acetyl-CoA determined at 2.7 A resolution |
| 2.3.1.82 | in complex with sisomicin |
| 2.3.1.82 | meta-AAC0020 enzyme mutant Y138A in complex with sisomicin, sitting drop vapor diffusion method, using 20% (w/v) PEG3350, 0.2 M calcium acetate. The apoenzyme is crystallized in a solution containing 4 M sodium formate |
| 2.3.1.82 | recombinant enzyme, vapor diffusion under oil, CoA-ribostamycin ternary complex |
| 2.3.1.82 | small-angle X-ray scattering analysis shows that the enzyme adopts a rigid conformation in solution, where the N-terminal acetyltransferase domain is fixed to the C-terminal phosphotransferase domain and not loosely tethered. The addition of acetyl-coenzyme A, coenzyme A, GDP, guanosine 5'-[beta,gamma-imido]triphosphate, and combinations thereof to the protein result in only modest changes to the radius of gyration of the enzyme, which are not consistent with any large changes in enzyme structure upon binding. These results imply some selective advantage to the bifunctional enzyme beyond coexpression as a single polypeptide, likely linked to an improvement in enzymatic properties. The rigid structure may contribute to improved electrostatic steering of aminoglycoside substrates toward the two active sites, which may provide such an advantage |
| 2.3.1.82 | structure of AAC(6')-Ig in complex with tobramycin reveals a large substrate-binding cleft remaining partially unoccupied by the substrate |
| 2.3.1.82 | structure of the kanamycin A complex of AAC(6')-Im. The substrate binds in a shallow positively-charged pocket, with the N6' amino group positioned appropriately for an efficient nucleophilic attack on an acetyl-CoA cofactor. Comparison of fortimicin binding to AAC(6')-Im and AAC(6')-Ie |
| 2.3.1.82 | structure of the N-terminal AAC(6')-Ie enzyme as a ternary kanamycin/coenzyme A abortive complex, to 1,3 A resolution. The AAC(6')-Ie enzyme is joined to the APH(2'')-Ia domain by a short, predominantly rigid linker at the N-terminal end of a long alpha-helix. The presence of the intact alpha-helix is essential to the activity of both functionalities of the full-length AAC(6')-Ie-APH(2'')-Ia enzyme. The two aminoglycoside-binding sites on the bifunctional enzyme are widely separated from each other |
| 2.3.1.82 | the structure of AAC(6')-Ib is determined in various complexes with donor and acceptor ligands to resolutions greater than 2.2 A |
