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NMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus.
European Biophysics Journal ( IF 2 ) Pub Date : 2020-03-09 , DOI: 10.1007/s00249-020-01428-x
Alexander Golubev 1, 2 , Bulat Fatkhullin 1, 3 , Azat Gabdulkhakov 3 , Aydar Bikmullin 1 , Liliya Nurullina 1 , Natalia Garaeva 1 , Daut Islamov 1 , Evelina Klochkova 1 , Vladimir Klochkov 4 , Albert Aganov 4 , Iskander Khusainov 1, 2, 5 , Shamil Validov 1 , Gulnara Yusupova 2 , Marat Yusupov 1, 2 , Konstantin Usachev 1, 4
Affiliation  

Elongation factor P (EF-P) is a translation protein factor that plays an important role in specialized translation of consecutive proline amino acid motifs. EF-P is an essential protein for cell fitness in native environmental conditions. It regulates synthesis of proteins involved in bacterial motility, environmental adaptation and bacterial virulence, thus making EF-P a potential drug target. In the present study, we determined the solution and crystal structure of EF-P from the pathogenic bacteria Staphylococcus aureus at 1.48 Å resolution. The structure can serve as a platform for structure-based drug design of novel antibiotics to combat the growing antibiotic resistance of S. aureus.

中文翻译:

核磁共振和晶体结构研究金黄色葡萄球菌的延伸因子P。

延伸因子P(EF-P)是一种翻译蛋白因子,在连续脯氨酸氨基酸基序的专门翻译中起重要作用。EF-P是天然环境条件下细胞适应性所必需的蛋白质。它调节涉及细菌运动性,环境适应性和细菌毒性的蛋白质的合成,因此使EF-P成为潜在的药物靶标。在本研究中,我们以1.48Å的分辨率确定了来自病原细菌金黄色葡萄球菌的EF-P的溶液和晶体结构。该结构可以用作新型抗生素基于结构的药物设计的平台,以对抗金黄色葡萄球菌不断增长的抗生素耐药性。
更新日期:2020-04-21
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