Crystal structure of a novel ATPase RadD from Escherichia coli

• Published in: Proteins, structure, function, and bioinformatics Vol. 87; no. 9; pp. 791 - 795
• Main Authors: Kuang, Xiaolin, Tang, Qun, Liu, Yan‐Ping, Yan, Xiao‐Xue, Xu, Wenqing
• Format: Journal Article
• Language: English
• Published: Hoboken, USA John Wiley & Sons, Inc 01.09.2019; Wiley Subscription Services, Inc
• Subjects: Adenosine triphosphatase; Adenosine Triphosphatases - genetics; Adenosine Triphosphatases - metabolism; ATPase RadD protein; Bacteria; Chromatography, Gel; Crystal structure; Deoxyribonucleic acid; DNA; DNA helicase; DNA repair; Domains; E coli; Escherichia coli; Escherichia coli - metabolism; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; helicase superfamily 2 proteins; Metabolism; Protein Binding; Protein Structure, Secondary; Proteins; RecA protein; RecA‐like domain; Ribonucleic acid; RNA; SF2 motifs; X‐ray crystallography; Zinc; zinc finger motif; Zinc finger proteins; X-ray crystallography; helicase superfamily 2 proteins; RecA-like domain; ATPase RadD protein; zinc finger motif; DNA repair; SF2 motifs
• ISSN: 0887-3585; 1097-0134
• DOI: 10.1002/prot.25704

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.