EC Number   |
Reference |
|---|
  1.8.4.11 | - |
684984 |
| 1.8.4.11 | 1-Cys type selenoprotein MsrA at 1.61.8 A, including the reduced, oxidized (sulfenic acid), and substrate-bound forms. The overall structure folds into a catalytic domain and a helical domain absent from other known MsrA structures. The side chain length of residue Glu55 is critical for its proton donor function |
741763 |
| 1.8.4.11 | 15-50 mg/ml purified recombinant MsrA in 50 mM Tris-HCl, pH 8.0, 2 mM EDTA, and 10 mM DTT, hanging drop vapour diffusion method, droplet size is 0.004-0.008 ml, equal volumes of protein and precipitant solution, X-ray diffraction structure determination and analysis at 1.9 A resolution |
667034 |
| 1.8.4.11 | crystals are obtained using the microbatch-under-oil method, four structures of the MsrA domain of the PilB protein from Neisseria meningitidis, representative of four catalytic intermediates of the MsrA catalytic cycle, are determined by X-ray crystallography |
688406 |
| 1.8.4.11 | molecular modeling. The conserved residue Glu99 is buried in the Met-S-(O) groove, which might contribute to the correct placing of substrates. Residue Asp134 does not form hydrogen bonds with the substrates but only within the enzyme |
742367 |
| 1.8.4.11 | single crystals of recombinant N-terminally 10His-tagged enzyme MsrA complexed with protein-bound methionine, hanging drop method, 30 mg/ml protein in 25 mM Tris-HCl, pH 8.0, 1 mM EDTA, 1 mM tris(carboxyethyl)phosphine hydrochloride, precipitant solution contains 2.0 M sodium formate, 0.1 M sodium citrate, pH 6.0, 4°C, 1 week, prior to data collection, crystals are soaked in 6.3 M sodium formate, 0.1 M sodium citrate, pH 6.0, for 2 min, and are flash-cooled, X-ray diffraction structure determination and analysis at 1.5 A resolution, polycrystalline clusters are obtained by sitting drop vapor diffusion method |
659028 |
| 1.8.4.11 | sitting drop vapor diffusion method, crystal structure of HpMsrAB C44S/C318S at 2.2 A, which shows that a linker region (Hpiloop, 193-205) between two domains interacts with each HpMsrA or HpMsrB domain via three salt bridges (E193-K107, D197-R103, and K200-D339) |
763911 |
| 1.8.4.11 | structure of dimeric MsrA to 2.9 A resolution, having the dimer interface around the two catalytic Cys16 residues. A central cone-shaped hole is present in the surface model of dimeric structure, and the two Cys16 residues constitute the base of the hole |
743579 |
| 1.8.4.11 | three-dimensional structure of MsrA in complex with AcMetSONHMe obtained by X-ray crystallography |
684715 |
| 1.8.4.11 | to 2.3 A resolution, in presence and absence of dithiothreitol |
741934 |
