2GXB

Crystal Structure of The Za Domain bound to Z-RNA

Summary for 2GXB

• Entry DOI: 10.2210/pdb2gxb/pdb
• Related: 1QBJ 1QJP 1XMK
• Descriptor: 5'-R(P*(DU)P*CP*GP*CP*GP*CP*G)-3', Double-stranded RNA-specific adenosine deaminase, SODIUM ION, ... (4 entities in total)
• Functional Keywords: z-rna, za, adar1, rna editing, protein-rna complex, hydrolase-rna complex, hydrolase/rna
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P55265
• Total number of polymer chains: 4
• Total formula weight: 19092.78

Authors

Athanasiadis, A.,Placido, D.,Rich, A. (deposition date: 2006-05-08, release date: 2007-05-01, Last modification date: 2023-08-30)

Primary citation

Placido, D.,Brown, B.A.,Lowenhaupt, K.,Rich, A.,Athanasiadis, A.
A Left-Handed RNA Double Helix Bound by the Zalpha Domain of the RNA-Editing Enzyme ADAR1.
Structure, 15:395-404, 2007

PubMed Abstract: The A form RNA double helix can be transformed to a left-handed helix, called Z-RNA. Currently, little is known about the detailed structural features of Z-RNA or its involvement in cellular processes. The discovery that certain interferon-response proteins have domains that can stabilize Z-RNA as well as Z-DNA opens the way for the study of Z-RNA. Here, we present the 2.25 A crystal structure of the Zalpha domain of the RNA-editing enzyme ADAR1 (double-stranded RNA adenosine deaminase) complexed to a dUr(CG)(3) duplex RNA. The Z-RNA helix is associated with a unique solvent pattern that distinguishes it from the otherwise similar conformation of Z-DNA. Based on the structure, we propose a model suggesting how differences in solvation lead to two types of Z-RNA structures. The interaction of Zalpha with Z-RNA demonstrates how the interferon-induced isoform of ADAR1 could be targeted toward selected dsRNAs containing purine-pyrimidine repeats, possibly of viral origin.

PubMed: 17437712
DOI: 10.1016/j.str.2007.03.001

Experimental method

X-RAY DIFFRACTION (2.25 Å)