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== '''Mechanism'' ==
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== '''Mechanism''' ==
DNA Gyrase works by introducing conformational changes to itself as well as the protein complex. The Gyrase enzyme begins by interacting with the DNA. This causes the formation of the three gates that can be opened and closed. The G-segment, introduced under the “structure” section, forms a bond and binds to the first of the 3 gates, the central DNA gate. This binding of the gate produces chiral wrapping which in then produces a T-segment with in the last of the 3 gates, the N gate. After which, the N-gate binds with ATP which then causes the gate to close. Once this process is completed, the G-segment is released from the last of the 3 gates, the C-gate. This process causes a net result of 2 negative supercoils and a linkage difference of 2 from the initial linkage.
DNA Gyrase works by introducing conformational changes to itself as well as the protein complex. The Gyrase enzyme begins by interacting with the DNA. This causes the formation of the three gates that can be opened and closed. The G-segment, introduced under the “structure” section, forms a bond and binds to the first of the 3 gates, the central DNA gate. This binding of the gate produces chiral wrapping which in then produces a T-segment with in the last of the 3 gates, the N gate. After which, the N-gate binds with ATP which then causes the gate to close. Once this process is completed, the G-segment is released from the last of the 3 gates, the C-gate. This process causes a net result of 2 negative supercoils and a linkage difference of 2 from the initial linkage.

Revision as of 00:46, 5 May 2017

DNA Gyrase

Caption for this structure

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== References == Schoeffler, A. J., May, A. P., & Berger, J. M. (2010). A domain insertion in Escherichia coli GyrB adopts a novel fold that plays a critical role in gyrase function. Nucleic Acids Research, 38(21), 7830-7844. doi:10.1093/nar/gkq665

Rahimi, H., Najafi, A., Eslami, H., Negahdari, B., & Moghaddam, M. M. (2016). Identification of novel bacterial DNA gyrase inhibitors: An in silico study. Journal Of Research In Pharmaceutical Sciences, 11(3), 250-258.

Travers, A., & Muskhelishvili, G. (2015). DNA structure and function. FEBS Journal, 282(12), 2279-2295. doi:10.1111/febs.13307

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