6N1R
Tetrahedral oligomeric complex of GyrA N-terminal fragment, solved by cryoEM in tetrahedral symmetry
Summary for 6N1R
| Entry DOI | 10.2210/pdb6n1r/pdb |
| Related | 6N1P 6N1Q |
| EMDB information | 9316 9317 9318 |
| Descriptor | DNA gyrase subunit A (1 entity in total) |
| Functional Keywords | topoisomerase, oligomeric complex, gyrase, isomerase |
| Biological source | Streptococcus pneumoniae G54 |
| Total number of polymer chains | 12 |
| Total formula weight | 695730.94 |
| Authors | Soczek, K.M.,Grant, T.,Rosenthal, P.B.,Mondragon, A. (deposition date: 2018-11-10, release date: 2018-12-05, Last modification date: 2024-03-20) |
| Primary citation | Soczek, K.M.,Grant, T.,Rosenthal, P.B.,Mondragon, A. CryoEM structures of open dimers of Gyrase A in complex with DNA illuminate mechanism of strand passage. Elife, 7:-, 2018 Cited by PubMed 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. PubMed: 30457554DOI: 10.7554/eLife.41215 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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