3PIO

Crystal structure of the synergistic antibiotic pair lankamycin and lankacidin in complex with the large ribosomal subunit

3PIO の概要

• エントリーDOI: 10.2210/pdb3pio/pdb
• 関連するPDBエントリー: 1NKW 1SM1 1YI2 2ZJR 3JQ4 3PIP
• 分子名称: RIBOSOMAL 23S RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (34 entities in total)
• 機能のキーワード: ribosome, large ribosomal subunit, 50s, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, trna-binding, lankamycin, lankacidin, macrolide, ribosome-antibiotic complex, ribosome/antibiotic
• 由来する生物種: Deinococcus radiodurans R1; 詳細
• タンパク質・核酸の鎖数: 30
• 化学式量合計: 1370433.47

構造登録者

Belousoff, M.J.,Shapira, T.,Bashan, A.,Zimmerman, E.,Arakawa, K.,Kinashi, H.,Rozenberg, H.,Yonath, A. (登録日: 2010-11-07, 公開日: 2011-02-23, 最終更新日: 2024-11-06)

主引用文献

Belousoff, M.J.,Shapira, T.,Bashan, A.,Zimmerman, E.,Rozenberg, H.,Arakawa, K.,Kinashi, H.,Yonath, A.
Crystal structure of the synergistic antibiotic pair, lankamycin and lankacidin, in complex with the large ribosomal subunit.
Proc.Natl.Acad.Sci.USA, 108:2717-2722, 2011

PubMed Abstract: The structures of the large ribosomal subunit of Deinococcus radiodurans (D50S) in complex with the antibiotic lankamycin (3.2 Å) and a double antibiotic complex of lankamycin and lankacidin C (3.45 Å) have been determined, in continuation of previous crystallographic studies on lankacidin-D50S complex. These two drugs have been previously reported to inhibit ribosomal function with mild synergistic effect. Lankamycin, a member of the macrolide family, binds in a similar manner to erythromycin. However, when in complex with lankacidin, lankamycin is located so that it can form interactions with lankacidin in the adjacent ribosomal binding site. When compared to the well-documented synergistic antibiotics, Streptogramins A and B, the pair of lankacidin and lankamycin bind in similar sites, the peptidyl transferase center and nascent peptide exit tunnel, respectively. Herein, we discuss the structural basis for antibiotic synergism and highlight the key factors involved in ribosomal inhibition.

PubMed: 21282615
DOI: 10.1073/pnas.1019406108

実験手法

X-RAY DIFFRACTION (3.2473 Å)