1J75

Crystal Structure of the DNA-Binding Domain Zalpha of DLM-1 Bound to Z-DNA

Summary for 1J75

• Entry DOI: 10.2210/pdb1j75/pdb
• Descriptor: 5'-D(*TP*CP*GP*CP*GP*CP*G)-3', Tumor Stroma and Activated Macrophage Protein DLM-1 (3 entities in total)
• Functional Keywords: protein-z-dna complex, immune system-dna complex, immune system/dna
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 2
• Total formula weight: 9442.85

Authors

Schwartz, T.,Behlke, J.,Lowenhaupt, K.,Heinemann, U.,Rich, A. (deposition date: 2001-05-15, release date: 2001-09-01, Last modification date: 2023-08-16)

Primary citation

Schwartz, T.,Behlke, J.,Lowenhaupt, K.,Heinemann, U.,Rich, A.
Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins.
Nat.Struct.Biol., 8:761-765, 2001

PubMed 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.

PubMed: 11524677
DOI: 10.1038/nsb0901-761

Experimental method

X-RAY DIFFRACTION (1.85 Å)