1KD1

Co-crystal Structure of Spiramycin bound to the 50S Ribosomal Subunit of Haloarcula marismortui

1KD1 の概要

• エントリーDOI: 10.2210/pdb1kd1/pdb
• 関連するPDBエントリー: 1K73 1K8A 1K9M 1KC8 1M1K
• 分子名称: 23S RRNA, RIBOSOMAL PROTEIN L10E, RIBOSOMAL PROTEIN L13, ... (37 entities in total)
• 機能のキーワード: 50s subunit, spiramycin, antibiotic, macrolide, carbinolamine, ribosome
• 由来する生物種: Haloarcula marismortui; 詳細
• タンパク質・核酸の鎖数: 30
• 化学式量合計: 1459062.96

構造登録者

Hansen, J.L.,Ippolito, J.A.,Ban, N.,Nissen, P.,Moore, P.B.,Steitz, T.A. (登録日: 2001-11-12, 公開日: 2002-07-19, 最終更新日: 2023-08-16)

主引用文献

Hansen, J.L.,Ippolito, J.A.,Ban, N.,Nissen, P.,Moore, P.B.,Steitz, T.A.
The structures of four macrolide antibiotics bound to the large ribosomal subunit.
Mol.Cell, 10:117-128, 2002

PubMed Abstract: Crystal structures of the Haloarcula marismortui large ribosomal subunit complexed with the 16-membered macrolide antibiotics carbomycin A, spiramycin, and tylosin and a 15-membered macrolide, azithromycin, show that they bind in the polypeptide exit tunnel adjacent to the peptidyl transferase center. Their location suggests that they inhibit protein synthesis by blocking the egress of nascent polypeptides. The saccharide branch attached to C5 of the lactone rings extends toward the peptidyl transferase center, and the isobutyrate extension of the carbomycin A disaccharide overlaps the A-site. Unexpectedly, a reversible covalent bond forms between the ethylaldehyde substituent at the C6 position of the 16-membered macrolides and the N6 of A2103 (A2062, E. coli). Mutations in 23S rRNA that result in clinical resistance render the binding site less complementary to macrolides.

PubMed: 12150912
DOI: 10.1016/S1097-2765(02)00570-1

実験手法

X-RAY DIFFRACTION (3 Å)