Structural basis of chiral wrap and T-segment capture by Escherichia coli DNA gyrase
Elizabeth Michalczyk, Zuzanna Pakosz-Stępień, Jonathon D. Liston, Olivia Gittins, Marta Pabis, Jonathan G. Heddle, Dmitry Ghilarov · 2024
Read Structural basis of chiral wrap and T-segment capture by Escherichia coli DNA gyrase by Elizabeth Michalczyk, Zuzanna Pakosz-Stępień, Jonathon D. Liston, Olivia Gittins, Marta Pabis, Jonathan G. Heddle, Dmitry Ghilarov (2024) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-11626157.txt.
Description
DNA gyrase is a bacterial enzyme that spends ATP energy to coil DNA negatively, a trick needed for copying and reading genes. Its proposed cycle traps a loop of DNA, passes one segment through a cut in another, and flips the sign of the coil, but the loop itself had never been seen. The seven authors captured high-resolution cryoEM structures of the Escherichia coli enzyme holding a chirally wrapped 217 base pair DNA, with and without the drug moxifloxacin.
Both structures show a positive figure-of-eight loop steadied by a flat, disc-like domain of the enzyme. Comparing the drug-free and drug-bound catalytic sites, each with a single metal ion, shows the enzyme frozen in a native state before the cut. The data imply the passing segment is trapped only after strand passage, not by the ATPase domains closing first.
Catalog record
| CREATOR | Elizabeth Michalczyk, Zuzanna Pakosz-Stępień, Jonathon D. Liston, Olivia Gittins, Marta Pabis, Jonathan G. Heddle, Dmitry Ghilarov |
|---|---|
| YEAR | 2024 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 50 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |