PMID:16226927

Citation	Sasaki, K, Ose, T, Tanaka, T, Mizukoshi, T, Ishigaki, T, Maenaka, K, Masai, H and Kohda, D (2006) Crystallization and preliminary crystallographic analysis of the N-terminal domain of PriA from Escherichia coli. Biochim. Biophys. Acta 1764:157-60
Abstract	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.
Links	PubMed Online version:10.1016/j.bbapap.2005.09.007
Keywords	Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Binding Sites; Crystallization; Crystallography, X-Ray; DNA Helicases/chemistry; DNA Helicases/genetics; DNA Helicases/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Oligodeoxyribonucleotides/chemistry; Oligodeoxyribonucleotides/metabolism; Peptide Fragments/chemistry; Peptide Fragments/genetics; Peptide Fragments/metabolism; Protein Structure, Tertiary; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/metabolism
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