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Science 11 June 1999:
Vol. 284. no. 5421, pp. 1841 - 1845
DOI: 10.1126/science.284.5421.1841

Reports

Crystal Structure of the Zalpha Domain of the Human Editing Enzyme ADAR1 Bound to Left-Handed Z-DNA

Thomas Schwartz, 1 Mark A. Rould, 2 Ky Lowenhaupt, 1 Alan Herbert, 1 Alexander Rich 1*

The editing enzyme double-stranded RNA adenosine deaminase includes a DNA binding domain, Zalpha , which is specific for left-handed Z-DNA. The 2.1 angstrom crystal structure of Zalpha complexed to DNA reveals that the substrate is in the left-handed Z conformation. The contacts between Zalpha 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 Zalpha to contact Z-DNA.

1 Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
2 Department of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405, USA.
*   To whom correspondence should be addressed.


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