4V7Y

Structure of the Thermus thermophilus 70S ribosome complexed with azithromycin.

これはPDB形式変換不可エントリーです。

4V7Y の概要

• エントリーDOI: 10.2210/pdb4v7y/pdb
• 関連するPDBエントリー: 3OGE 3OGY 3OH5 3OH7 3OHC 3OHD 3OHJ 3OHK 3OI2 3OI3 3OI4 3OI5
• 分子名称: 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (55 entities in total)
• 機能のキーワード: ribosome, protein synthesis, azithromycin, ribosome-antibiotic complex, ribosome/antibiotic
• 由来する生物種: Thermus thermophilus; 詳細
• タンパク質・核酸の鎖数: 102
• 化学式量合計: 4267390.57

構造登録者

Bulkley, D.P.,Innis, C.A.,Blaha, G.,Steitz, T.A. (登録日: 2010-08-18, 公開日: 2014-07-09, 最終更新日: 2024-11-06)

主引用文献

Bulkley, D.,Innis, C.A.,Blaha, G.,Steitz, T.A.
Revisiting the structures of several antibiotics bound to the bacterial ribosome.
Proc.Natl.Acad.Sci.USA, 107:17158-17163, 2010

PubMed Abstract: The increasing prevalence of antibiotic-resistant pathogens reinforces the need for structures of antibiotic-ribosome complexes that are accurate enough to enable the rational design of novel ribosome-targeting therapeutics. Structures of many antibiotics in complex with both archaeal and eubacterial ribosomes have been determined, yet discrepancies between several of these models have raised the question of whether these differences arise from species-specific variations or from experimental problems. Our structure of chloramphenicol in complex with the 70S ribosome from Thermus thermophilus suggests a model for chloramphenicol bound to the large subunit of the bacterial ribosome that is radically different from the prevailing model. Further, our structures of the macrolide antibiotics erythromycin and azithromycin in complex with a bacterial ribosome are indistinguishable from those determined of complexes with the 50S subunit of Haloarcula marismortui, but differ significantly from the models that have been published for 50S subunit complexes of the eubacterium Deinococcus radiodurans. Our structure of the antibiotic telithromycin bound to the T. thermophilus ribosome reveals a lactone ring with a conformation similar to that observed in the H. marismortui and D. radiodurans complexes. However, the alkyl-aryl moiety is oriented differently in all three organisms, and the contacts observed with the T. thermophilus ribosome are consistent with biochemical studies performed on the Escherichia coli ribosome. Thus, our results support a mode of macrolide binding that is largely conserved across species, suggesting that the quality and interpretation of electron density, rather than species specificity, may be responsible for many of the discrepancies between the models.

PubMed: 20876130
DOI: 10.1073/pnas.1008685107

実験手法

X-RAY DIFFRACTION (3 Å)