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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary crystallographic studies of Sfp: a phosphopantetheinyl transferase of modular peptide synthetases.
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Crystallization and preliminary crystallographic studies of Sfp: a phosphopantetheinyl transferase of modular peptide synthetases.

机译：结晶和初步的晶体研究Sfp: phosphopantetheinyl转移酶模块化的肽合成酶。

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摘要

The Bacillus subtilis Sfp protein is required for the non-ribosomal biosynthesis of the lipoheptapeptide antibiotic surfactin. It converts seven peptidyl carrier protein (PCP) domains of the surfactin synthetase SfrA-(A-C) to their active holo-forms by 4'-phosphopantetheinylation. The B. subtilis sfp gene was overexpressed in Escherichia coli and its gene product was purified to homogeneity and crystallized. Well diffracting single crystals were obtained from Sfp as well as from a selenomethionyl derivative, using sodium formate as a precipitant. The crystals belong to the tetragonal space group P41212/P43212, with unit-cell parameters a = b = 65.3, c = 150.5 A. They diffract beyond 2.8 A and contain one molecule in the asymmetric unit.
机译：枯草芽孢杆菌Sfp蛋白质的需要non-ribosomal生物合成的lipoheptapeptide抗生素surfactin。将七肽基载体蛋白(PCP)域的surfactin合成酶SfrA - (a - c)他们的活跃holo-forms4“-phosphopantetheinylation。基因在大肠杆菌中,其基因产物纯化和同质性结晶。从Sfp以及获得的吗selenomethionyl导数,用甲酸钠作为沉淀剂。正方空间群P41212 / P43212,晶胞参数a = b = 65.3, c = 150.5。他们衍射超出2.8,包含一个分子在不对称单位。

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