1YIT

Crystal Structure Of Virginiamycin M and S Bound To The 50S Ribosomal Subunit Of Haloarcula Marismortui

1YIT の概要

• エントリーDOI: 10.2210/pdb1yit/pdb
• 関連するPDBエントリー: 1KHR 1N8R 1YHQ 1YI2 1YIJ 1YJ9
• 関連するBIRD辞書のPRD_ID: PRD_000227
• 分子名称: 23S RIBOSOMAL RNA, 50S RIBOSOMAL PROTEIN L5P, 50S RIBOSOMAL PROTEIN L6P, ... (38 entities in total)
• 機能のキーワード: virginiamycin m, virginiamycin s, peptidyl transferase, ribosome, streptogramin, ribosome-antibiotic complex, antibiotic, cyclohexadepsipeptide, ribosome/antibiotic
• 由来する生物種: HALOARCULA MARISMORTUI; 詳細
• タンパク質・核酸の鎖数: 32
• 化学式量合計: 1481914.32

構造登録者

Tu, D.,Blaha, G.,Moore, P.B.,Steitz, T.A. (登録日: 2005-01-13, 公開日: 2005-04-26, 最終更新日: 2024-10-09)

主引用文献

TU, D.,Blaha, G.,Moore, P.B.,Steitz, T.A.
Structures of Mlsbk Antibiotics Bound to Mutated Large Ribosomal Subunits Provide a Structural Explanation for Resistance.
Cell(Cambridge,Mass.), 121:257-, 2005

PubMed Abstract: Crystal structures of H. marismortui large ribosomal subunits containing the mutation G2099A (A2058 in E. coli) with erythromycin, azithromycin, clindamycin, virginiamycin S, and telithromycin bound explain why eubacterial ribosomes containing the mutation A2058G are resistant to them. Azithromycin binds almost identically to both G2099A and wild-type subunits, but the erythromycin affinity increases by more than 10(4)-fold, implying that desolvation of the N2 of G2099 accounts for the low wild-type affinity for macrolides. All macrolides bind similarly to the H. marismortui subunit, but their binding differs significantly from what has been reported in the D. radioidurans subunit. The synergy in the binding of streptogramins A and B appears to result from a reorientation of the base of A2103 (A2062, E. coli) that stacks between them. The structure of large subunit containing a three residue deletion mutant of L22 shows a change in the L22 structure and exit tunnel shape that illuminates its macrolide resistance phenotype.

PubMed: 15851032
DOI: 10.1016/J.CELL.2005.02.005

実験手法

X-RAY DIFFRACTION (2.8 Å)