Language

English

Publication Date

4-20-2026

Journal

Nature Communications

DOI

10.1038/s41467-026-71884-0

PMID

42009660

PMCID

PMC13284261

PubMedCentral® Posted Date

4-20-2026

PubMedCentral® Full Text Version

Post-print

Abstract

To understand how gyrase interacts with DNA and selects a site of action, we created an ad hoc shape-based recognition methodology to ascertain the DNA sequence from cryoEM density maps as a string of purines and pyrimidines, which matched to the DNA minicircle sequence in our two previous cryoEM structures of negatively supercoiled DNA bound to E. coli gyrase. For one structure, the Gate- or G-segment sequence contains base-pair steps that are among the most flexible in the minicircle, facilitating the bend. The sequence flanking this G-segment is highly inflexible, preventing wrapping the β-pinwheel of gyrase. In the other structure, a flexible DNA minicircle sequence wraps a β-pinwheel of gyrase and the G-segment contains base-pair steps of average deformability. This work highlights how DNA sequence and deformability impact gyrase. It also demonstrates the utility of both identifying DNA sequences from cryoEM structures and assessing base-pair step deformability.

Keywords

DNA Gyrase, Escherichia coli, Cryoelectron Microscopy, DNA, Bacterial, Nucleic Acid Conformation, DNA, Superhelical, Models, Molecular, Base Sequence, Cryoelectron microscopy, Computational biophysics, DNA

Published Open-Access

yes

Share

COinS
 
 

To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.