TY - JOUR
T1 - Crystallization and preliminary crystallographic analysis of the N-terminal domain of PriA from Escherichia coli
AU - Sasaki, Kaori
AU - Ose, Toyoyuki
AU - Tanaka, Taku
AU - Mizukoshi, Toshimi
AU - Ishigaki, Tomoko
AU - Maenaka, Katsumi
AU - Masai, Hisao
AU - Kohda, Daisuke
PY - 2006/1/1
Y1 - 2006/1/1
N2 - 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.
AB - 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.
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U2 - 10.1016/j.bbapap.2005.09.007
DO - 10.1016/j.bbapap.2005.09.007
M3 - Article
C2 - 16226927
AN - SCOPUS:33644834103
VL - 1764
SP - 157
EP - 160
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
SN - 1570-9639
IS - 1
ER -