ArticleeLife2018
CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage.
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Sequence-encoded determinants of regional mutational plasticity: comparative analysis of PE_PGRS genes in Mycobacterium tuberculosis and other bacteria.Scientific reports · 2026Article
- Structural and Computational Analysis ofBiomolecules · 2026Article
- Structural and Computational Analysis ofbioRxiv : the preprint server for biology · 2025Article
- Different propensities for gate opening in gyrases and topoisomerase IV.Nucleic acids research · 2025Article
- Structural basis of chiral wrap and T-segment capture byProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structures of African swine fever virus topoisomerase complex and their implications.Nature communications · 2024Article
- Signal Propagation in the ATPase Domain ofBiochemistry · 2024Article
- Structure-function analysis of the ATPase domain of African swine fever virus topoisomerase.mBio · 2024Article
- A unified view on enzyme catalysis by cryo-EM study of a DNA topoisomerase.Communications chemistry · 2024Article
- Friend or Foe: Protein Inhibitors of DNA Gyrase.Biology · 2024Review
- What's on the Other Side of the Gate: A Structural Perspective on DNA Gate Opening of Type IA and IIA DNA Topoisomerases.International journal of molecular sciences · 2023Review
- Intracellular Experimental Evolution ofACS infectious diseases · 2023Article
- DNA Gyrase as a Target for Quinolones.Biomedicines · 2023Review
- Molecular mechanism of topoisomerase poisoning by the peptide antibiotic albicidin.Nature catalysis · 2023Article
- Expanded Dataset Reveals the Emergence and Evolution of DNA Gyrase in Archaea.Molecular biology and evolution · 2022Article
- Escherichia coli GyrA Tower Domain Interacts with QnrB1 Loop B and Plays an Important Role in QnrB1 Protection from Quinolone Inhibition.Antimicrobial agents and chemotherapy · 2021Article
- Structural basis for allosteric regulation of Human Topoisomerase IIα.Nature communications · 2021Article
- Natural and Synthetic Oligoarylamides: Privileged Structures for Medical Applications.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Review
- Protein Side-Chain-DNA Contacts Probed by Fast Magic-Angle Spinning NMR.The journal of physical chemistry. B · 2020Article
- Structure-Function Analysis Reveals the Singularity of Plant Mitochondrial DNA Replication Components: A Mosaic and Redundant System.Plants (Basel, Switzerland) · 2019Review
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Authors and funding
4 authors.
Funding
Abstract
Gyrase is a unique type IIA topoisomerase that uses ATP hydrolysis to maintain the negatively supercoiled state of bacterial DNA. In order to perform its function, gyrase undergoes a sequence of conformational changes that consist of concerted gate openings, DNA cleavage, and DNA strand passage events. Structures where the transported DNA molecule (T-segment) is trapped by the A subunit have not been observed. Here we present the cryoEM structures of two oligomeric complexes of open gyrase A dimers and DNA. The protein subunits in these complexes were solved to 4 Å and 5.2 Å resolution. One of the complexes traps a linear DNA molecule, a putative T-segment, which interacts with the open gyrase A dimers in two states, representing steps either prior to or after passage through the DNA-gate. The structures locate the T-segment in important intermediate conformations of the catalytic cycle and provide insights into gyrase-DNA interactions and mechanism.
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