9I5T9I5T の概要
| エントリーDOI | 10.2210/pdb9i5t/pdb |
| EMDBエントリー | 52635 |
| 分子名称 | Large ribosomal subunit protein bL28, 23S rRNA, 5S rRNA, ... (38 entities in total) |
| 機能のキーワード | ribosome, antibiotics, macrolide-resistance |
| 由来する生物種 | Porphyromonas gingivalis 詳細 |
| タンパク質・核酸の鎖数 | 32 |
| 化学式量合計 | 1381236.13 |
| 構造登録者 | |
| 主引用文献 | Hiregange, D.G.,Samiya, S.,Mizgalska, D.,Ben-Zeev, E.,Waghalter, M.,Rivalta, A.,Rajan, K.S.,Halfon, Y.,Breiner-Goldstein, E.,Kaczmarczyk, I.,Sroka, A.,Taoka, M.,Nobe, Y.,Isobe, T.,Paukner, S.,Zimmerman, E.,Bashan, A.,Potempa, J.,Yonath, A. Structural studies of ribosome from an anaerobic Bacteroidetes human pathogen Porphyromonas gingivalis. Nucleic Acids Res., 53:-, 2025 Cited by PubMed Abstract: Porphyromonas gingivalis, an anaerobic pathogen in chronic periodontitis, belongs to the Bacteroidota phylum and is associated with various virulence factors. Its antibiotic-resistant strains and its propensity to form biofilms pose a challenge to effective treatment. To explore therapeutic avenues, we studied the high-resolution cryogenic electron microscope structures of ribosomes from the wild-type P. gingivalis W83 and the macrolide-resistant mutant strain ermΔporN. The structural analysis revealed unique features primarily at the ribosome periphery. Together with the distinctive distribution of ribosomal RNA modifications, these findings offer insights into the therapeutical potential, such as creation of novel therapeutic compounds inhibiting the specific cellular functions of the P. gingivalis ribosomes. Moreover, the high-resolution structure of the ermΔporN ribosome in its complex with the approved antibiotic lefamulin suggests its repurposing against P. gingivalis. Furthermore, we provide a foundation for additional effective strategies to treat periodontitis and associated systemic diseases. PubMed: 40444637DOI: 10.1093/nar/gkaf458 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.6 Å) |
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