Cryo-EM structure of HflX bound to the Listeria monocytogenes 50S ribosomal subunit
Ontology highlight
ABSTRACT:
SUBMITTER: Timm Oliver Koller
PROVIDER: EMPIAR-12112 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural basis for HflXr-mediated antibiotic resistance in Listeria monocytogenes.
Koller Timm O TO Turnbull Kathryn J KJ Vaitkevicius Karolis K Crowe-McAuliffe Caillan C Roghanian Mohammad M Bulvas Ondřej O Nakamoto Jose A JA Kurata Tatsuaki T Julius Christina C Atkinson Gemma C GC Johansson Jörgen J Hauryliuk Vasili V Wilson Daniel N DN
Nucleic acids research 20221001 19
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 over ...[more]
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