6ENH

Crystal structure of the 43K ATPase domain of Thermus thermophilus gyrase B in complex with an aminocoumarin

Summary for 6ENH

Entry DOI	10.2210/pdb6enh/pdb
Descriptor	DNA gyrase subunit B, Coumermycin A1, IMIDAZOLE, ... (4 entities in total)
Functional Keywords	topoisomerase, gyrase b-aminocoumarin complex, isomerase
Biological source	Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Total number of polymer chains	1
Total formula weight	44249.01
Authors	Vanden Broeck, A.,McEwen, A.G.,Lamour, V. (deposition date: 2017-10-04, release date: 2019-04-10, Last modification date: 2024-01-17)
Primary citation	Vanden Broeck, A.,McEwen, A.G.,Chebaro, Y.,Potier, N.,Lamour, V. Structural Basis for DNA Gyrase Interaction with Coumermycin A1. J.Med.Chem., 62:4225-4231, 2019 Cited by PubMed Abstract: Coumermycin A1 is a natural aminocoumarin that inhibits bacterial DNA gyrase, a member of the GHKL proteins superfamily. We report here the first cocrystal structures of gyrase B bound to coumermycin A1, revealing that one coumermycin A1 molecule traps simultaneously two ATP-binding sites. The inhibited dimers from different species adopt distinct sequence-dependent conformations, alternative to the ATP-bound form. These structures provide a basis for the rational development of coumermycin A1 derivatives for antibiotherapy and biotechnology applications. PubMed: 30920824 DOI: 10.1021/acs.jmedchem.8b01928 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.94 Å)

Structure validation