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- W2008364078 abstract "DNA gyrase is unique among enzymes for its ability to actively introduce negative supercoils into DNA. This function is mediated in part by the C-terminal domain of its A subunit (GyrA CTD). Here, we report the crystal structure of this ≈35-kDa domain determined to 1.75-Å resolution. The GyrA CTD unexpectedly adopts an unusual fold, which we term a β-pinwheel, that is globally reminiscent of a β-propeller but is built of blades with a previously unobserved topology. A large, conserved basic patch on the outer edge of this domain suggests a likely site for binding and bending DNA; fluorescence resonance energy transfer-based assays show that the GyrA CTD is capable of bending DNA by ≥180° over a 40-bp region. Surprisingly, we find that the CTD of the topoisomerase IV A subunit, which shares limited sequence homology with the GyrA CTD, also bends DNA. Together, these data provide a physical explanation for the ability of DNA gyrase to constrain a positive superhelical DNA wrap, and also suggest that the particular substrate preferences of topoisomerase IV might be dictated in part by the function of this domain." @default.
- W2008364078 created "2016-06-24" @default.
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- W2008364078 creator A5026504117 @default.
- W2008364078 creator A5039868655 @default.
- W2008364078 date "2004-05-03" @default.
- W2008364078 modified "2023-10-11" @default.
- W2008364078 title "The C-terminal domain of DNA gyrase A adopts a DNA-bending β-pinwheel fold" @default.
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- W2008364078 doi "https://doi.org/10.1073/pnas.0401595101" @default.
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