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首页> 外文期刊>Biochimica et biophysica acta. Biomembranes >Biophysical characterization and stabilization of detergent-solubilized lipoprotein N-acyl transferase from P-aeruginosa and E-coli
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Biophysical characterization and stabilization of detergent-solubilized lipoprotein N-acyl transferase from P-aeruginosa and E-coli

机译：P-eruginosa和E-Coli的洗涤剂 - 溶解脂蛋白N-酰基转移酶的生物物理表征及稳定性

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摘要

Lipoproteins are important for bacterial growth and virulence and interest in them as targets for antibiotic development is growing. Lipoprotein N-acyl transferase (Lnt) catalyzes the final step in the lipoprotein post-translational processing pathway. The mature lipoprotein can remain in the inner membrane or be trafficked to the outer membrane in the case of diderm prokaryotes. With a view to obtaining high-resolution crystal structures of membrane integral Lnt for use in drug discovery a program was undertaken to generate milligram quantities of stable, homogenous and functional protein. This involved screening across bacterial species for suitable orthologues and optimization at the level of protein expression, solubilization and stability. Combining biophysical and functional characterization, orthologous Lnt from Escherichia coli and the opportunistic human pathogen Pseudomonas aeruginosa was identified as suitable for the proposed structure determination campaign that ultimately yielded crystal structures. The rational approaches taken that eventually provided structure-quality protein are presented in this report.
机译：脂蛋白对于细菌生长和毒力和毒力以及抗生素发育的目标是重要的。脂蛋白N-酰基转移酶（LNT）催化脂蛋白后翻译加工途径的最终步骤。成熟的脂蛋白可以保留在内膜中，或者在DEDERM原核生物的情况下被贩运到外膜。为了获得用于药物发现的膜整体LNT的高分辨率晶体结构，进行了一种程序，以产生毫克稳定，均匀和功能性蛋白质。这涉及在蛋白质表达，溶解和稳定性水平下筛选跨细菌物种和优化。从大肠杆菌和机会人体病原体假单胞菌铜绿假单胞菌结合了生物物理和功能表征，从大肠杆菌和机会人体病原体铜绿假单胞菌被鉴定为适用于最终产生晶体结构的建议结构确定运动。本报告中提出了最终提供了结构质量蛋白的合理方法。

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