Abstract
The editing enzyme double-stranded RNA adenosine deaminase includes a DNA binding domain, Zα, which is specific for left-handed Z-DNA. The 2.1 angstrom crystal structure of Zα complexed to DNA reveals that the substrate is in the left-handed Z conformation. The contacts between Zα and Z-DNA are made primarily with the “zigzag” sugar-phosphate backbone, which provides a basis for the specificity for the Z conformation. A single base contact is observed to guanine in the syn conformation, characteristic of Z-DNA. Intriguingly, the helix-turn-helix motif, frequently used to recognize B-DNA, is used by Zα to contact Z-DNA.
References
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Dates
Type | When |
---|---|
Created | 23 years ago (July 27, 2002, 5:49 a.m.) |
Deposited | 1 year, 7 months ago (Jan. 13, 2024, 4:06 a.m.) |
Indexed | 3 weeks, 3 days ago (July 30, 2025, 11:21 a.m.) |
Issued | 26 years, 2 months ago (June 11, 1999) |
Published | 26 years, 2 months ago (June 11, 1999) |
Published Print | 26 years, 2 months ago (June 11, 1999) |
@article{Schwartz_1999, title={Crystal Structure of the Zα Domain of the Human Editing Enzyme ADAR1 Bound to Left-Handed Z-DNA}, volume={284}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.284.5421.1841}, DOI={10.1126/science.284.5421.1841}, number={5421}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Schwartz, Thomas and Rould, Mark A. and Lowenhaupt, Ky and Herbert, Alan and Rich, Alexander}, year={1999}, month=jun, pages={1841–1845} }