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Crystal structure of a novel ATPase RadD from Escherichia coli
Author(s) -
Kuang Xiaolin,
Tang Qun,
Liu YanPing,
Yan XiaoXue,
Xu Wenqing
Publication year - 2019
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25704
Subject(s) - helicase , escherichia coli , aaa proteins , atpase , dna , zinc finger , biology , computational biology , gene , rna helicase a , microbiology and biotechnology , rna , genetics , chemistry , biochemistry , enzyme , transcription factor
Abstract The helicase superfamily 2 (SF2) proteins are involved in essentially every step in DNA and RNA metabolism. The radD ( yejH ) gene, which belongs to SF2, plays an important role in DNA repair. The RadD protein includes all seven conserved SF2 motifs and has shown ATPase activity. Here, we first reported the structure of RadD from Escherichia coli containing two RecA‐like domains, a zinc finger motif, and a C‐terminal domain. Based on the structure of RadD and other SF2 proteins, we then built a model of the RedD‐ATP complex.

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