6N1Q

Dihedral oligomeric complex of GyrA N-terminal fragment, solved by cryoEM in D2 symmetry

Summary for 6N1Q

• Entry DOI: 10.2210/pdb6n1q/pdb
• Related: 6N1P 6N1R
• 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: 8
• Total formula weight: 463820.62

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

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: 30457554
DOI: 10.7554/eLife.41215

Experimental method

ELECTRON MICROSCOPY (5.16 Å)