Crystallization and preliminary X-ray analysis of an Escherichia coli purine repressor-hypoxanthine-DNA complex.
Crystallization and preliminary X-ray analysis of an Escherichia coli purine repressor-hypoxanthine-DNA complex.
复制标题
大肠杆菌嘌呤阻遏物-次黄嘌呤-DNA 复合物的结晶和初步 X 射线分析。
DOI：
10.1006/jmbi.1994.1580
复制
发表时间：
1994
影响因子：
5.6
通讯作者：
Brennan,RG
中科院分区：
文献类型：
--
作者：
Schumacher,MA;Choi,KY;Zalkin,H;Brennan,RG
The purine repressor (PurR) is a DNA-binding protein, which together with a purine corepressor serves to regulatede novopurine and pyrimidine biosynthesis inEscherichia coli. PurR belongs to the structurally homologouslacrepressor family of transcription regulators. A PurR-hypoxanthine-DNA complex has been crystallized, with DNA encompassing the high affinitypurFoperator site and which is 16 base-pairs long with 5′-deoxynucleoside overhangs on each complementary strand. The crystals diffract to better than 2·6 Å and take the orthorhombic space groupC2221, with unit cell dimensionsa= 175·9 Å,b= 94·8 Å andc= 81·8 Å. The structure determination of this PurR-hypoxanthine-DNA complex will provide the first high resolution view of a Lacl member-DNA complex.
