1QBJ
CRYSTAL STRUCTURE OF THE ZALPHA Z-DNA COMPLEX
Summary for 1QBJ
Entry DOI | 10.2210/pdb1qbj/pdb |
Descriptor | DNA (5'-D(*TP*CP*GP*CP*GP*CP*G)-3'), PROTEIN (DOUBLE-STRANDED RNA SPECIFIC ADENOSINE DEAMINASE (ADAR1)) (3 entities in total) |
Functional Keywords | protein-z-dna complex, hydrolase-dna complex, hydrolase/dna |
Biological source | Homo sapiens (human) More |
Cellular location | Cytoplasm: P55265 |
Total number of polymer chains | 6 |
Total formula weight | 33350.07 |
Authors | Schwartz, T.,Rould, M.A.,Rich, A. (deposition date: 1999-04-22, release date: 1999-07-02, Last modification date: 2024-02-14) |
Primary citation | Schwartz, T.,Rould, M.A.,Lowenhaupt, K.,Herbert, A.,Rich, A. Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA. Science, 284:1841-1845, 1999 Cited by PubMed Abstract: 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. PubMed: 10364558DOI: 10.1126/science.284.5421.1841 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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