File:Reverse Gyrase Mechanism.jpg

Reverse_Gyrase_Mechanism.jpg(762 × 266 pixels, file size: 60 KB, MIME type: image/jpeg)

Summary

Description
English: The mechanism proposes that the initial binding of reverse gyrase to the DNA induces an unwinding of about 20 base pairs; after ATP binding, the bubble is rewound to about 10 base pairs, and the topoisomerase IA domain is able to introduce positive supercoils during strand passage. The enzyme is released from the DNA strand upon ATP hydrolysis, and the process can be repeated elsewhere along the DNA strand.
Date
Source https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7245102/figure/fig06/
Author Xi Yang, Florence Garnier, Hélène Débat, Terence R. Strick, and Marc Nadal

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Captions

Visual depiction of the proposed mechanism of action of the reverse gyrase enzyme with ATP hydrolysis.

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current18:35, 19 October 2022Thumbnail for version as of 18:35, 19 October 2022762 × 266 (60 KB)ClderieUploaded a work by Xi Yang, Florence Garnier, Hélène Débat, Terence R. Strick, and Marc Nadal from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7245102/figure/fig06/ with UploadWizard
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