1zi0: Difference between revisions

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[[Image:1zi0.gif|left|200px]]
{{Seed}}
[[Image:1zi0.png|left|200px]]


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{{STRUCTURE_1zi0|  PDB=1zi0  |  SCENE=  }}  
{{STRUCTURE_1zi0|  PDB=1zi0  |  SCENE=  }}  


'''A Superhelical Spiral in Escherichia coli DNA Gyrase A C-terminal Domain Imparts Unidirectional Supercoiling Bias'''
===A Superhelical Spiral in Escherichia coli DNA Gyrase A C-terminal Domain Imparts Unidirectional Supercoiling Bias===




==Overview==
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DNA gyrase is unique among type II topoisomerases in that its DNA supercoiling activity is unidirectional. The C-terminal domain of the gyrase A subunit (GyrA-CTD) is required for this supercoiling bias. We report here the x-ray structure of the Escherichia coli GyrA-CTD (Protein Data Bank code 1ZI0). The E. coli GyrA-CTD adopts a circular-shaped beta-pinwheel fold first seen in the Borrelia burgdorferi GyrA-CTD. However, whereas the B. burgdorferi GyrA-CTD is flat, the E. coli GyrA-CTD is spiral. DNA relaxation assays reveal that the E. coli GyrA-CTD wraps DNA inducing substantial (+) superhelicity, while the B. burgdorferi GyrA-CTD introduces a more modest (+) superhelicity. The observation of a superhelical spiral in the present structure and that of the Bacillus stearothermophilus ParC-CTD structure suggests unexpected similarities in substrate selectivity between gyrase and Topo IV enzymes. We propose a model wherein the right-handed ((+) solenoidal) wrapping of DNA around the E. coli GyrA-CTD enforces unidirectional (-) DNA supercoiling.
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{{ABSTRACT_PUBMED_15897198}}


==About this Structure==
==About this Structure==
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[[Category: Spiralling beta pinwheel]]
[[Category: Spiralling beta pinwheel]]
[[Category: Topoisomerase]]
[[Category: Topoisomerase]]
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