scholarly journals Evidence for a conformational change in the DNA gyrase–DNA complex from hydroxyl radical footprinting

1994 ◽  
Vol 22 (9) ◽  
pp. 1567-1575 ◽  
Author(s):  
George Orphanides ◽  
Anthony Maxwell
Keyword(s):  
Hydroxyl Radical ◽  
Conformational Change ◽  
Dna Gyrase ◽  
Hydroxyl Radical Footprinting ◽  
Dna Complex

scholarly journals Mapping Functionally Important Motifs SPF and GGQ of the Decoding Release Factor RF2 to theEscherichia coliRibosome by Hydroxyl Radical Footprinting

2002 ◽  
Vol 278 (17) ◽  
pp. 15095-15104 ◽  
Author(s):  
Debbie-Jane G. Scarlett ◽  
Kim K. McCaughan ◽  
Daniel N. Wilson ◽  
Warren P. Tate
Keyword(s):  
Hydroxyl Radical ◽  
Release Factor ◽  
Hydroxyl Radical Footprinting

scholarly journals Quinolones: Mechanism, Lethality and Their Contributions to Antibiotic Resistance

Molecules ◽  
2020 ◽  
Vol 25 (23) ◽  
pp. 5662
Author(s):  
Natassja G. Bush ◽  
Isabel Diez-Santos ◽  
Lauren R. Abbott ◽  
Anthony Maxwell
Keyword(s):  
Cell Death ◽  
Antibiotic Resistance ◽  
Dna Gyrase ◽  
Mechanisms Of Action ◽  
Quinolone Resistance ◽  
Topoisomerase Iv ◽  
Bacterial Enzymes ◽  
Dna Topoisomerase ◽  
Quinolone Antibiotics ◽  
Dna Complex

Fluoroquinolones (FQs) are arguably among the most successful antibiotics of recent times. They have enjoyed over 30 years of clinical usage and become essential tools in the armoury of clinical treatments. FQs target the bacterial enzymes DNA gyrase and DNA topoisomerase IV, where they stabilise a covalent enzyme-DNA complex in which the DNA is cleaved in both strands. This leads to cell death and turns out to be a very effective way of killing bacteria. However, resistance to FQs is increasingly problematic, and alternative compounds are urgently needed. Here, we review the mechanisms of action of FQs and discuss the potential pathways leading to cell death. We also discuss quinolone resistance and how quinolone treatment can lead to resistance to non-quinolone antibiotics.

scholarly journals Structural interpretation of DNA–protein hydroxyl-radical footprinting experiments with high resolution using HYDROID

2018 ◽  
Vol 13 (11) ◽  
pp. 2535-2556 ◽  
Author(s):  
Alexey K. Shaytan ◽  
Hua Xiao ◽  
Grigoriy A. Armeev ◽  
Daria A. Gaykalova ◽  
Galina A. Komarova ◽  
...  
Keyword(s):  
High Resolution ◽  
Hydroxyl Radical ◽  
Structural Interpretation ◽  
Hydroxyl Radical Footprinting

scholarly journals Ligand-induced Conformational Shift in the N-terminal Domain of GRP94, an Hsp90 Chaperone

2004 ◽  
Vol 279 (44) ◽  
pp. 46162-46171 ◽  
Author(s):  
Robert M. Immormino ◽  
D. Eric Dollins ◽  
Paul L. Shaffer ◽  
Karen L. Soldano ◽  
Melissa A. Walker ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Crystal Structures ◽  
Conformational Change ◽  
Atp Hydrolysis ◽  
Dna Gyrase ◽  
Regulatory Domain ◽  
Conformational Switch ◽  
Terminal Ligand ◽  
Conformational Rearrangement ◽  
Hsp90 Chaperone

GRP94 is the endoplasmic reticulum paralog of cytoplasmic Hsp90. Models of Hsp90 action posit an ATP-dependent conformational switch in the N-terminal ligand regulatory domain of the chaperone. However, crystal structures of the isolated N-domain of Hsp90 in complex with a variety of ligands have yet to demonstrate such a conformational change. We have determined the structure of the N-domain of GRP94 in complex with ATP, ADP, and AMP. Compared with theN-ethylcarboxamidoadenosine and radicicol-bound forms, these structures reveal a large conformational rearrangement in the protein. The nucleotide-bound form exposes new surfaces that interact to form a biochemically plausible dimer that is reminiscent of those seen in structures of MutL and DNA gyrase. Weak ATP binding and a conformational change in response to ligand identity are distinctive mechanistic features of GRP94 and suggest a model for how GRP94 functions in the absence of co-chaperones and ATP hydrolysis.

Analyzing the structure of macromolecules in their native cellular environment using hydroxyl radical footprinting

The Analyst ◽  
2018 ◽  
Vol 143 (4) ◽  
pp. 798-807 ◽  
Author(s):  
Emily E. Chea ◽  
Lisa M. Jones
Keyword(s):  
Nucleic Acids ◽  
Hydroxyl Radical ◽  
Live Cells ◽  
Cellular Environment ◽  
Hydroxyl Radical Footprinting

Hydroxyl radical footprinting (HRF) has been successfully used to study the structure of both nucleic acids and proteins in live cells.

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