大肠杆菌PriA蛋白N端结构域的结晶及初步晶体学分析

Crystallization and preliminary crystallographic analysis of the N-terminal domain of PriA from Escherichia coli.

作者信息

Sasaki Kaori, Ose Toyoyuki, Tanaka Taku, Mizukoshi Toshimi, Ishigaki Tomoko, Maenaka Katsumi, Masai Hisao, Kohda Daisuke

机构信息

Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan.

出版信息

Biochim Biophys Acta. 2006 Jan;1764(1):157-60. doi: 10.1016/j.bbapap.2005.09.007. Epub 2005 Oct 3.

DOI:10.1016/j.bbapap.2005.09.007

PMID:16226927

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.

摘要

PriA是一种DEXH型DNA解旋酶，通过其N端结构域特异性结合DNA的3'末端，是一种识别细菌中停滞的DNA复制叉的候选传感蛋白。我们在不存在和存在寡核苷酸的情况下，使PriA的N端片段结晶，以阐明特异性识别DNA 3'末端的结构基础。