6S0Z

Erythromycin Resistant Staphylococcus aureus 50S ribosome (delta R88 A89 uL22) in complex with erythromycin.

これはPDB形式変換不可エントリーです。

6S0Z の概要

• エントリーDOI: 10.2210/pdb6s0z/pdb
• EMDBエントリー: 10077
• 分子名称: 23S ribosomal RNA, 50S ribosomal protein L15, 50S ribosomal protein L16, ... (31 entities in total)
• 機能のキーワード: ribosome, antibiotics, resistance, staphylococcus aureus, exit tunnel, rna, rproteins, erythromycin
• 由来する生物種: Staphylococcus aureus; 詳細
• タンパク質・核酸の鎖数: 30
• 化学式量合計: 1325387.24

構造登録者

Halfon, Y.,Matozv, D.,Eyal, Z.,Bashan, A.,Zimmerman, E.,Kjeldgaard, J.,Ingmer, H.,Yonath, A. (登録日: 2019-06-18, 公開日: 2019-08-21, 最終更新日: 2024-10-16)

主引用文献

Halfon, Y.,Matzov, D.,Eyal, Z.,Bashan, A.,Zimmerman, E.,Kjeldgaard, J.,Ingmer, H.,Yonath, A.
Exit tunnel modulation as resistance mechanism of S. aureus erythromycin resistant mutant.
Sci Rep, 9:11460-11460, 2019

PubMed Abstract: The clinical use of the antibiotic erythromycin (ery) is hampered owing to the spread of resistance genes that are mostly mutating rRNA around the ery binding site at the entrance to the protein exit tunnel. Additional effective resistance mechanisms include deletion or insertion mutations in ribosomal protein uL22, which lead to alterations of the exit tunnel shape, located 16 Å away from the drug's binding site. We determined the cryo-EM structures of the Staphylococcus aureus 70S ribosome, and its ery bound complex with a two amino acid deletion mutation in its ß hairpin loop, which grants the bacteria resistance to ery. The structures reveal that, although the binding of ery is stable, the movement of the flexible shorter uL22 loop towards the tunnel wall creates a wider path for nascent proteins, thus enabling bypass of the barrier formed by the drug. Moreover, upon drug binding, the tunnel widens further.

PubMed: 31391518
DOI: 10.1038/s41598-019-48019-1

実験手法

ELECTRON MICROSCOPY (2.3 Å)