Crystal structure of a novel ATPase RadD from Escherichia coli

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 report...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2019-09, Vol.87 (9), p.791-795
Hauptverfasser:	Kuang, Xiaolin, Tang, Qun, Liu, Yan‐Ping, Yan, Xiao‐Xue, Xu, Wenqing
Format:	Artikel
Sprache:	eng
Schlagworte:	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
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	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.
ISSN:	0887-3585 1097-0134
DOI:	10.1002/prot.25704