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首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Refolding purification and crystallization of the FrpB outer membrane iron transporter from Neisseria meningitidis
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Refolding purification and crystallization of the FrpB outer membrane iron transporter from Neisseria meningitidis

机译：脑膜炎奈瑟氏球菌FrpB外膜铁转运蛋白的重折叠纯化和结晶

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摘要

FrpB is an integral outer membrane protein from the human pathogen Neisseria meningitidis. It is a member of the TonB-dependent transporter family and promotes the uptake of iron across the outer membrane. There is also evidence that FrpB is an antigen and hence a potential component of a vaccine against meningococcal meningitis. FrpB incorporating a polyhistidine tag was overexpressed in Escherichia coli into inclusion bodies. The protein was then solubilized in urea, refolded and purified to homogeneity. Two separate antigenic variants of FrpB were crystallized by sitting-drop vapour diffusion. Crystals of the F5-1 variant diffracted to 2.4 Å resolution and belonged to space group C2, with unit-cell parameters a = 176.5, b = 79.4, c = 75.9 Å, β = 98.3°. Crystal-packing calculations suggested the presence of a monomer in the asymmetric unit. Crystals of the F3-3 variant also diffracted to 2.4 Å resolution and belonged to space group P212121, with unit-cell parameters a = 85.3, b = 104.6, c = 269.1 Å. Preliminary analysis suggested the presence of an FrpB trimer in the asymmetric unit.
机译：FrpB是一种来自人类病原体脑膜炎奈瑟氏球菌的外膜蛋白。它是依赖于TonB的转运蛋白家族的成员，并促进整个外膜吸收铁。也有证据表明FrpB是一种抗原，因此是抗脑膜炎球菌性脑膜炎疫苗的潜在成分。掺入多组氨酸标签的FrpB在大肠杆菌中过表达成包涵体。然后将蛋白质溶解在尿素中，重新折叠并纯化至均质。 FrpB的两个单独的抗原变异体通过坐滴式蒸汽扩散进行结晶。 F5-1变体的晶体衍射至2.4？Å的分辨率，属于C2空间群，其晶胞参数a = 176.5，b = 79.4，c = 75.9，β= 98.3°。晶体堆积计算表明不对称单元中存在单体。 F3-3变体的晶体也衍射到2.4Å分辨率，并属于空间群P212121，其晶胞参数a = 85.3，b = 104.6，c = 269.1。初步分析表明在不对称单元中存在FrpB三聚体。

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