8A63

Cryo-EM structure of Listeria monocytogenes 50S ribosomal subunit.

8A63 の概要

• エントリーDOI: 10.2210/pdb8a63/pdb
• 関連するPDBエントリー: 7NHN
• EMDBエントリー: 12334 15204
• 分子名称: 50S ribosomal protein L28, 23S ribosomal RNA, 5S ribosomal RNA, ... (34 entities in total)
• 機能のキーワード: ribosome, listeria monocytogenes, 50s
• 由来する生物種: Listeria monocytogenes EGD-e; 詳細
• タンパク質・核酸の鎖数: 29
• 化学式量合計: 1341133.01

構造登録者

Koller, T.O.,Crowe-McAuliffe, C.,Wilson, D.N. (登録日: 2022-06-16, 公開日: 2022-11-02, 最終更新日: 2024-11-20)

主引用文献

Koller, T.O.,Turnbull, K.J.,Vaitkevicius, K.,Crowe-McAuliffe, C.,Roghanian, M.,Bulvas, O.,Nakamoto, J.A.,Kurata, T.,Julius, C.,Atkinson, G.C.,Johansson, J.,Hauryliuk, V.,Wilson, D.N.
Structural basis for HflXr-mediated antibiotic resistance in Listeria monocytogenes.
Nucleic Acids Res., 50:11285-11300, 2022

PubMed Abstract: HflX is a ubiquitous bacterial GTPase that splits and recycles stressed ribosomes. In addition to HflX, Listeria monocytogenes contains a second HflX homolog, HflXr. Unlike HflX, HflXr confers resistance to macrolide and lincosamide antibiotics by an experimentally unexplored mechanism. Here, we have determined cryo-EM structures of L. monocytogenes HflXr-50S and HflX-50S complexes as well as L. monocytogenes 70S ribosomes in the presence and absence of the lincosamide lincomycin. While the overall geometry of HflXr on the 50S subunit is similar to that of HflX, a loop within the N-terminal domain of HflXr, which is two amino acids longer than in HflX, reaches deeper into the peptidyltransferase center. Moreover, unlike HflX, the binding of HflXr induces conformational changes within adjacent rRNA nucleotides that would be incompatible with drug binding. These findings suggest that HflXr confers resistance using an allosteric ribosome protection mechanism, rather than by simply splitting and recycling antibiotic-stalled ribosomes.

PubMed: 36300626
DOI: 10.1093/nar/gkac934

実験手法

ELECTRON MICROSCOPY (3.1 Å)