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Structural and functional studies of a large winged Z‐ DNA ‐binding domain of Danio rerio protein kinase PKZ
Author(s) -
Subramani Vinod Kumar,
Kim Doyoun,
Yun Kyunghee,
Kim Kyeong Kyu
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12238
Subject(s) - danio , dna , zebrafish , hmg box , dna binding domain , binding domain , binding site , dna binding protein , biology , chemistry , biochemistry , stereochemistry , gene , transcription factor
The Z‐ DNA ‐binding domain of PKZ from zebrafish ( Danio rerio ; drZα PKZ ) contains the largest β‐wing among known Z‐ DNA ‐binding domains. To elucidate the functional implication of the β‐wing, we solved the crystal structure of apo‐drZα PKZ . Structural comparison with its Z‐ DNA ‐bound form revealed a large conformational change within the β‐wing during Z‐ DNA binding. Biochemical studies of protein mutants revealed that two basic residues in the β‐wing are responsible for Z‐ DNA recognition as well as fast B–Z transition. Therefore, the extra basic residues in the β‐wing of drZα PKZ are necessary for the fast B–Z transition activity.