Cryo-EM structure of the ribosome functional complex of the human pathogenStaphylococcus aureusat 3.2 Å resolution

被引:10
|
作者
Golubev, Alexander [1 ,2 ]
Fatkhullin, Bulat [1 ,3 ]
Khusainov, Iskander [1 ,4 ]
Jenner, Lasse [2 ]
Gabdulkhakov, Azat [1 ,3 ]
Validov, Shamil [1 ]
Yusupova, Gulnara [2 ]
Yusupov, Marat [1 ,2 ]
Usachev, Konstantin [1 ]
机构
[1] Kazan Fed Univ, Inst Fundamental Med & Biol, Lab Struct Biol, 18 Kremlyovskaya, Kazan 420008, Russia
[2] Univ Strasbourg, Inst Genet & Biol Mol & Cellulaire, Dept Biol & Genom Struct, CNRS UMR7104,INSERM U964, Illkirch Graffenstaden, France
[3] Russian Acad Sci, Inst Prot Res, Pushchino, Russia
[4] Max Planck Inst Biophys, Dept Mol Sociol, Frankfurt, Germany
基金
俄罗斯科学基金会;
关键词
antibiotic resistance; drug targets; methyltransferases; ribosome; rRNA modifications; Staphylococcus aureus; X-RAY ANALYSIS; ESCHERICHIA-COLI; TRANSFER-RNA; MESSENGER-RNA; BACTERIAL RIBOSOME; PROTEIN-SYNTHESIS; CRYSTAL-STRUCTURE; 70S RIBOSOME; METHYLTRANSFERASE; 16S;
D O I
10.1002/1873-3468.13915
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Staphylococcus aureusis a bacterial pathogen and one of the leading causes of healthcare-acquired infections in the world. The growing antibiotic resistance ofS. aureusobliges us to search for new drugs and treatments. As the majority of antibiotics target the ribosome, knowledge of its detailed structure is crucial for drug development. Here, we report the cryo-EM reconstruction at 3.2 angstrom resolution of theS. aureusribosome with P-site tRNA, messenger RNA, and 10 RNA modification sites previously not assigned or visualized. The resulting model is the most precise and complete high-resolution structure to date of theS. aureus70S ribosome with functional ligands.
引用
收藏
页码:3551 / 3567
页数:17
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