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首页> 外文期刊>Acta Crystallographica Section F >Purification, crystallization and preliminary X-ray diffraction analysis of Cif, a virulence factor secreted by Pseudomonas aeruginosa
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Purification, crystallization and preliminary X-ray diffraction analysis of Cif, a virulence factor secreted by Pseudomonas aeruginosa

机译：铜绿假单胞菌分泌的毒力因子Cif的纯化，结晶和初步X射线衍射分析

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摘要

The opportunistic pathogen Pseudomonas aeruginosa secretes a protein that triggers the accelerated degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) in airway epithelial cells. This protein, which is known as the CFTR inhibitory factor (Cif), acts as a virulence factor and may facilitate airway colonization by P. aeruginosa. Based on sequence similarity Cif appears to be an epoxide hydrolase (EH), but it lacks several of the conserved features found in the active sites of canonical members of the EH family. Here, the crystallization of purified recombinant Cif by vapor diffusion is reported. The crystals formed in space group C2, with unit-cell parameters a = 167.4, b = 83.6, c = 88.3 Å, β = 100.6° . The crystals diffracted to 2.39 Å resolution on a rotating-anode source. Based on the calculated Matthews coefficient (2.2 Å3 Da−1), it appears that the asymmetric unit contains four molecules.
机译：机会病原体铜绿假单胞菌分泌一种蛋白质，该蛋白质触发气道上皮细胞中的囊性纤维化跨膜电导调节剂（CFTR）加速降解。这种蛋白质被称为CFTR抑制因子（Cif），可作为一种毒力因子，可促进铜绿假单胞菌在气道中的定殖。基于序列相似性，Cif似乎是一种环氧水解酶（EH），但缺乏EH家族经典成员活性位点中发现的一些保守特征。在此，报道了通过蒸气扩散纯化的重组Cif的结晶。在空间群C2中形成的晶体，其晶胞参数a = 167.4，b = 83.6，c = 88.3，β= 100.6°。晶体在旋转阳极源上衍射至2.39Å分辨率。根据计算出的马修斯系数（2.2Å 3 Da -1 ），看来不对称单元包含四个分子。

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