DNA gyrase subunit B (GyrB) (GyrB)

DNA gyrase subunit B (GyrB) is a fundamental bacterial enzyme in Escherichia coli, belonging to the Type II topoisomerase family [UniProt: P0AES6]. It functions as the ATPase component of the A2B2 heterotetrameric DNA gyrase complex, providing the energy required to introduce negative supercoils into double-stranded DNA [PubMed: PMC4914131]. This activity is essential for relieving torsional strain during DNA replication and transcription, ensuring the proper progression of the replication fork [NCBI: NBK545253]. Because DNA gyrase is vital for bacterial viability and lacks a direct human counterpart, it is a highly validated target for antimicrobial agents [PubMed: 24513171]. Aminocoumarin antibiotics, such as novobiocin, bind to the ATP-binding site of GyrB, thereby inhibiting its catalytic function and halting bacterial growth [PubChem: CID 5467576]. Recent pharmaceutical research focuses on developing novel GyrB inhibitors to combat the rising threat of multi-drug resistant bacteria, particularly those resistant to fluoroquinolones [Journal of Medicinal Chemistry: 10.1021/jm501713u].

Other names

GyrBDNA topoisomerase II subunit BDNA topoisomerase 2 subunit BEscherichia coli DNA gyrase B

Inhibition of the ATPase activity of the GyrB subunit, which prevents the enzyme from utilizing ATP hydrolysis to drive the negative supercoiling of DNA, ultimately leading to the cessation of bacterial DNA replication and cell death.