7C0I

Crystal structure of chimeric mutant of E3L in complex with Z-DNA

Summary for 7C0I

• Entry DOI: 10.2210/pdb7c0i/pdb
• Descriptor: Double-stranded RNA-binding protein,Double-stranded RNA-specific adenosine deaminase, DNA (5'-D(*TP*CP*GP*CP*GP*CP*G)-3'), SULFATE ION, ... (4 entities in total)
• Functional Keywords: e3l, protein-dna complex, protein engineering, z-dna binding protein, dna binding protein
• Biological source: Vaccinia virus; More
• Total number of polymer chains: 6
• Total formula weight: 33881.20

Authors

Choi, H.J.,Park, C.H.,Kim, J.S. (deposition date: 2020-05-01, release date: 2020-12-16, Last modification date: 2023-11-29)

Primary citation

Park, C.,Zheng, X.,Park, C.Y.,Kim, J.,Lee, S.K.,Won, H.,Choi, J.,Kim, Y.G.,Choi, H.J.
Dual conformational recognition by Z-DNA binding protein is important for the B-Z transition process.
Nucleic Acids Res., 48:12957-12971, 2020

PubMed Abstract: Left-handed Z-DNA is radically different from the most common right-handed B-DNA and can be stabilized by interactions with the Zα domain, which is found in a group of proteins, such as human ADAR1 and viral E3L proteins. It is well-known that most Zα domains bind to Z-DNA in a conformation-specific manner and induce rapid B-Z transition in physiological conditions. Although many structural and biochemical studies have identified the detailed interactions between the Zα domain and Z-DNA, little is known about the molecular basis of the B-Z transition process. In this study, we successfully converted the B-Z transition-defective Zα domain, vvZαE3L, into a B-Z converter by improving B-DNA binding ability, suggesting that B-DNA binding is involved in the B-Z transition. In addition, we engineered the canonical B-DNA binding protein GH5 into a Zα-like protein having both Z-DNA binding and B-Z transition activities by introducing Z-DNA interacting residues. Crystal structures of these mutants of vvZαE3L and GH5 complexed with Z-DNA confirmed the significance of conserved Z-DNA binding interactions. Altogether, our results provide molecular insight into how Zα domains obtain unusual conformational specificity and induce the B-Z transition.

PubMed: 33245772
DOI: 10.1093/nar/gkaa1115

Experimental method

X-RAY DIFFRACTION (2.4 Å)