Crystallization and preliminary crystallographic analysis of the N-terminal domain of PriA from Escherichia coli.
PriA, a DEXH-type DNA helicase, binds specifically to the 3' end of DNA through its N-terminal domain, and is a candidate sensor protein that recognizes arrested DNA replication forks in bacteria. We crystallized an N-terminal fragment of PriA in the absence and the presence of oligonucleotides to elucidate the structural basis for the specific recognition of the 3' terminus of DNA.
Sasaki
Kaori
K
Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan.
Ose
Toyoyuki
T
Tanaka
Taku
T
Mizukoshi
Toshimi
T
Ishigaki
Tomoko
T
Maenaka
Katsumi
K
Masai
Hisao
H
Kohda
Daisuke
D
D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D004265:DNA Helicases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins; D009838:Oligodeoxyribonucleotides / Q000737:chemistry / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D029968:Escherichia coli Proteins; D009838:Oligodeoxyribonucleotides; D010446:Peptide Fragments; D011994:Recombinant Proteins; D000251:Adenosine Triphosphatases; C506743:priA protein, E coli; D004265:DNA Helicases