Escherichia coli DNA gyrase subunit B (GyrB)

Escherichia coli DNA gyrase subunit B (GyrB) is an essential enzyme responsible for managing the topological state of DNA during replication, transcription, and repair. It functions as part of a heterotetrameric A2B2 complex, where GyrB provides the ATPase activity necessary to drive the introduction of negative supercoils into the bacterial chromosome (UniProt: P0AES6). This process is vital for relieving the torsional strain that accumulates ahead of the replication fork, ensuring efficient genomic duplication. Because GyrB is essential for bacterial viability and possesses a highly conserved ATP-binding site that differs significantly from human kinases and topoisomerases, it serves as an attractive target for antibiotic development (PubMed: 25853348). Traditional inhibitors like the aminocoumarin novobiocin compete with ATP for binding to GyrB, while newer agents like zoliflodacin target the subunit to overcome resistance seen with GyrA-targeting quinolones (PubMed: 28945376). Despite its potential, the clinical utility of GyrB inhibitors has historically been limited by toxicity and the rapid emergence of resistance, though next-generation inhibitors are currently in clinical trials for treating multi-drug resistant infections (PubMed: 21435141).

Other names

DNA gyrase subunit BGyrBDNA topoisomerase 2 subunit BTopoisomerase II subunit B

Inhibition of the ATPase activity of the GyrB subunit, which prevents the energy-dependent introduction of negative supercoils into DNA, leading to the arrest of DNA replication and bacterial cell death (PubMed: 25853348).