8KAB の概要
| エントリーDOI | 10.2210/pdb8kab/pdb |
| EMDBエントリー | 37007 |
| 分子名称 | 50S ribosomal protein bL37, 50S ribosomal protein L10, 50S ribosomal protein L11, ... (36 entities in total) |
| 機能のキーワード | complex, ribosome |
| 由来する生物種 | Mycolicibacterium smegmatis MC2 155 詳細 |
| タンパク質・核酸の鎖数 | 35 |
| 化学式量合計 | 1538269.80 |
| 構造登録者 | |
| 主引用文献 | Srinivasan, K.,Banerjee, A.,Sengupta, J. Cryo-EM structures reveal the molecular mechanism of HflX-mediated erythromycin resistance in mycobacteria. Structure, 32:1443-, 2024 Cited by PubMed Abstract: Mycobacterial HflX confers resistance against macrolide antibiotics. However, the exact molecular mechanism is poorly understood. To gain further insights, we determined the cryo-EM structures of M. smegmatis (Msm) HflX-50S subunit and 50S subunit-erythromycin (ERY) complexes at a global resolution of approximately 3 Å. A conserved nucleotide A2286 at the gate of nascent peptide exit tunnel (NPET) adopts a swayed conformation in HflX-50S complex and interacts with a loop within the linker helical (LH) domain of MsmHflX that contains an additional 9 residues insertion. Interestingly, the swaying of this nucleotide, which is usually found in the non-swayed conformation, is induced by erythromycin binding. Furthermore, we observed that erythromycin decreases HflX's ribosome-dependent GTP hydrolysis, resulting in its enhanced binding and anti-association activity on the 50S subunit. Our findings reveal how mycobacterial HflX senses the presence of macrolides at the peptide tunnel entrance and confers antibiotic resistance in mycobacteria. PubMed: 39029461DOI: 10.1016/j.str.2024.06.016 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.3 Å) |
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