"Crystallization and preliminary crystallographic analysis of nosiheptide-resistance methyltransferase from Streptomyces actuosus in complex with SAM."

Yang H, Wang P, Dong Z, Li X, Gong R, Yang Y, Li Z, Xu Y, Xu Y



Published 2010-05-01 in Acta Crystallogr Sect F Struct Biol Cryst Commun volume 66 .

Pubmed ID: 20445264
DOI identifier: -

Abstract:
Nosiheptide-resistance methyltransferase (NSR) methylates 23S rRNA at the nucleotide adenosine 1067 in Escherichia coli and thus contributes to resistance against nosiheptide, a sulfur-containing peptide antibiotic. Here, the expression, purification and crystallization of NSR from Streptomyces actuosus are reported. Diffracting crystals were grown by the hanging-drop vapour-diffusion method in reservoir solution consisting of 0.35 M ammonium chloride, 24%(w/v) PEG 3350, 0.1 M MES pH 5.7 at 293 K. Native data have been collected from the apo enzyme and a SAM complex, as well as apo SeMet SAD data. The diffraction patterns of the apo form of NSR, of NSR complexed with SAM and of SeMet-labelled NSR crystals extended to 1.90, 1.95 and 2.25 A resolution, respectively, using synchrotron radiation. All crystals belonged to space group P2(1), with approximate unit-cell parameters a = 64.6, b = 69.6, c = 64.9 A, beta = 117.8 degrees .


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Last modification of this entry: Sept. 6, 2012