期刊
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
卷 59, 期 5, 页码 2849-2854出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.04895-14
关键词
-
资金
- Bizkaia: Talent
- European Union's Seventh Framework Programme (Marie Curie actions [COFUND])
- Cluster of Excellence Macromolecular Complexes at Goethe University Frankfurt (DFG project) [EXC 115]
- Deutsche Forschungsgemeinschaft [FU579 1-3]
- Marie Curie career integration grant [PCIG14-GA-2013-632072]
Although both tetracycline and tigecycline inhibit protein synthesis by sterically hindering the binding of tRNA to the ribosomal A site, tigecycline shows increased efficacy in both in vitro and in vivo activity assays and escapes the most common resistance mechanisms associated with the tetracycline class of antibiotics. These differences in activities are attributed to the tert-butylglycylamido side chain found in tigecycline. Our structural analysis by X-ray crystallography shows that tigecycline binds the bacterial 30S ribosomal subunit with its tail in an extended conformation and makes extensive interactions with the 16S rRNA nucleotide C1054. These interactions restrict the mobility of C1054 and contribute to the antimicrobial activity of tigecycline, including its resistance to the ribosomal protection proteins.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据