6ENG
Crystal structure of the 43K ATPase domain of Escherichia coli gyrase B in complex with an aminocoumarin
Summary for 6ENG
| Entry DOI | 10.2210/pdb6eng/pdb |
| Descriptor | DNA gyrase subunit B, PHOSPHATE ION, TETRAETHYLENE GLYCOL, ... (8 entities in total) |
| Functional Keywords | topoisomerase, gyrase b-aminocoumarin complex, isomerase |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 2 |
| Total formula weight | 89468.89 |
| 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: 30920824DOI: 10.1021/acs.jmedchem.8b01928 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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