Summary information and primary citation

PDB-id
1j75; SNAP-derived features in text and JSON formats; DNAproDB
Class
immune system-DNA
Method
X-ray (1.85 Å)
Summary
Crystal structure of the DNA-binding domain zalpha of dlm-1 bound to z-DNA
Reference
Schwartz T, Behlke J, Lowenhaupt K, Heinemann U, Rich A (2001): "Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins." Nat.Struct.Biol., 8, 761-765. doi: 10.1038/nsb0901-761.
Abstract
The first crystal structure of a protein, the Z alpha high affinity binding domain of the RNA editing enzyme ADAR1, bound to left-handed Z-DNA was recently described. The essential set of residues determined from this structure to be critical for Z-DNA recognition was used to search the database for other proteins with the potential for Z-DNA binding. We found that the tumor-associated protein DLM-1 contains a domain with remarkable sequence similarities to Z alpha(ADAR). Here we report the crystal structure of this DLM-1 domain bound to left-handed Z-DNA at 1.85 A resolution. Comparison of Z-DNA binding by DLM-1 and ADAR1 reveals a common structure-specific recognition core within the binding domain. However, the domains differ in certain residues peripheral to the protein-DNA interface. These structures reveal a general mechanism of Z-DNA recognition, suggesting the existence of a family of winged-helix proteins sharing a common Z-DNA binding motif.

Cartoon-block schematics in six views (download the tarball)

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