Structural highlights
Function
[A0A0Y2BJX7_STREE] A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.[HAMAP-Rule:MF_01897]
Publication Abstract from PubMed
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 A and 5.16 A 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.
CryoEM structures of open dimers of Gyrase A in complex with DNA illuminate mechanism of strand passage.,Soczek KM, Grant T, Rosenthal PB, Mondragon A Elife. 2018 Nov 20;7. pii: 41215. doi: 10.7554/eLife.41215. PMID:30457554[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Soczek KM, Grant T, Rosenthal PB, Mondragon A. CryoEM structures of open dimers of Gyrase A in complex with DNA illuminate mechanism of strand passage. Elife. 2018 Nov 20;7. pii: 41215. doi: 10.7554/eLife.41215. PMID:30457554 doi:http://dx.doi.org/10.7554/eLife.41215
