Dataset Information
Escherichia coli gyrase holocomplex with 217 bp phage Mu SGS DNA and albicidin stabilised by ADPNP
Ontology highlight
ABSTRACT:
SUBMITTER: Dmitry Ghilarov
PROVIDER: EMPIAR-11244 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Molecular mechanism of topoisomerase poisoning by the peptide antibiotic albicidin.
Nature catalysis 20230123 1
The peptide antibiotic albicidin is a DNA topoisomerase inhibitor with low-nanomolar bactericidal activity towards fluoroquinolone-resistant Gram-negative pathogens. However, its mode of action is poorly understood. We determined a 2.6 Å resolution cryoelectron microscopy structure of a ternary complex between <i>Escherichia coli</i> topoisomerase DNA gyrase, a 217 bp double-stranded DNA fragment and albicidin. Albicidin employs a dual binding mechanism where one end of the molecule obstructs th ...[more]
