Nosiheptide is a member of the thiopeptide family of antibiotics which demonstrates potent activities against various bacterial pathogens. The formation of its C-terminal amide is catalysed by NosA in an unusual strategy for maturating certain thiopeptides by processing precursor peptides featuring a serine extension. Here, a recombinant C-terminally truncated selenomethionine-derivatized NosA(1-111) variant from Streptomyces actuosus consisting of residues 1-111, named SeMet NosA(1-111), was crystallized using the sitting-drop vapour-diffusion method. Diffraction data were collected to 2.40 angstrom resolution using synchrotron radiation. The crystals belonged to the primitive cubic space group P4(1)32, with unit-cell parameters a = b = c = 143.3 angstrom. Assuming the presence of three molecules in the asymmetric unit, the calculated Matthews coefficient was 3.94 angstrom(3)Da(-1) and the corresponding solvent content was 40.3%.
Wang YT,Liu SS,Me PF,et al. Crystallographic analysis of NosA, which catalyzes terminal amide formation in the biosynthesis of nosiheptide[J]. Acta Crystallogr. F-Struct. Biol. Commun.,2015,71:1033-1037.