PMID:15698572

Citation	Costenaro, L, Grossmann, JG, Ebel, C and Maxwell, A (2005) Small-angle X-ray scattering reveals the solution structure of the full-length DNA gyrase a subunit. Structure 13:287-96
Abstract	DNA gyrase is the topoisomerase uniquely able to actively introduce negative supercoils into DNA. Vital in all bacteria, but absent in humans, this enzyme is a successful target for antibacterial drugs. From biophysical experiments in solution, we report the low-resolution structure of the full-length A subunit (GyrA). Analytical ultracentrifugation shows that GyrA is dimeric, but nonglobular. Ab initio modeling from small-angle X-ray scattering allows us to retrieve the molecular envelope of GyrA and thereby the organization of its domains. The available crystallographic structure of the amino-terminal domain (GyrA59) forms a dimeric core, and two additional pear-shaped densities closely flank it in an unexpected position. Each accommodates very well a carboxyl-terminal domain (GyrA-CTD) built from a homologous crystallographic structure. The uniqueness of gyrase is due to the ability of the GyrA-CTDs to wrap DNA. Their position within the GyrA structure strongly suggests a large conformation change of the enzyme upon DNA binding.
Links	PubMed Online version:10.1016/j.str.2004.12.011
Keywords	Amino Acid Sequence; DNA Gyrase/chemistry; Dimerization; Escherichia coli/enzymology; Molecular Conformation; Molecular Sequence Data; Solutions/chemistry; Ultracentrifugation; X-Ray Diffraction
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