The C-terminal domain of DNA gyrase A adopts a DNA-bending -pinwheel fold
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The C-terminal domain of DNA gyrase A adopts a DNA-bending -pinwheel fold
of this Article Full Text of this Article Institution: Univ of California Sign In as Member / Individual Corbett et al. 10.1073/pnas.0401595101. Supporting Information Files in this Data Supplement: Supporting Table 1 Supporting Figure 5 Supporting Figure 6 Fig. 5. Sequence alignment between the CTDs of BbGac, E. coli GyrA (EcGyrA), and E. coli ParC (EcParC). Secondary structure of BbGac is sho...
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As only the type II topoisomerase is capable of introducing negative supercoiling, DNA gyrase is involved in crucial cellular processes. Although the other domains of DNA gyrase are better understood, the mechanism of DNA binding by the C-terminal domain of the DNA gyrase A subunit (GyrA-CTD) is less clear. Here, we investigated the DNA-binding sites in the GyrA-CTD of Mycobacterium tuberculosi...
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DNA gyrase subunit B C-terminal domain (GyrB-CTD) is a functional module of DNA gyrase which participates in forming the core of DNA gyrase and plays critical roles in G-segment binding and T-segment loading and passage. Here, the purification, crystallization and preliminary X-ray crystallographic studies of GyrB-CTD from Mycobacterium tuberculosis H37Rv are reported. Diffraction data were col...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2004
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0401595101