Crystal Structure of the Zα Domain of the Human Editing Enzyme ADAR1 Bound to Left-Handed Z-DNA-Reference-Cited by-同舟云学术

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

Published:1999-06-11 Issue:5421 Volume:284 Page:1841-1845
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Schwartz Thomas¹,Rould Mark A.²,Lowenhaupt Ky¹,Herbert Alan¹,Rich Alexander¹

Affiliation:

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.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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