2RVC: Solution structure of Zalpha domain of goldfish ZBP-containing protein kinase

Z-DNA binding proteins (ZBPs) play important roles in RNA editing, innate immune response and viral infection. Structural and biophysical studies show that ZBPs initially form an intermediate complex with B-DNA for B-Z conversion. However, a comprehensive understanding of the mechanism of Z-DNA binding and B-Z transition is still lacking, due to the absence of structural information on the intermediate complex. Here, we report the solution structure of the Zalpha domain of the ZBP-containing protein kinase from Carassius auratus(caZalphaPKZ). We quantitatively determined the binding affinity of caZalphaPKZ for both B-DNA and Z-DNA and characterized its B-Z transition activity, which is modulated by varying the salt concentration. Our results suggest that the intermediate complex formed by caZalphaPKZ and B-DNA can be used as molecular ruler, to measure the degree to which DNA transitions to the Z isoform.
PDB ID: 2RVCDownload
MMDB ID: 136112
PDB Deposition Date: 2015/7/8
Updated in MMDB: 2017/06
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2RVC: monomeric; determined by author
Molecular Components in 2RVC
Label Count Molecule
Protein (1 molecule)
Interferon-inducible and Double-stranded-dependent Eif-2kinase
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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