THE PHAGE-434 CRO/OR1 COMPLEX AT 2.5A RESOLUTION

被引:134
作者
MONDRAGON, A
HARRISON, SC
机构
[1] HARVARD UNIV,HOWARD HUGHES MED INST,CAMBRIDGE,MA 02138
[2] HARVARD UNIV,DEPT BIOCHEM & MOLEC BIOL,CAMBRIDGE,MA 02138
关键词
DNA RECOGNITION; DNA CONFORMATION; HELIX-TURN-HELIX; REPRESSOR; X-RAY CRYSTALLOGRAPHY;
D O I
10.1016/0022-2836(91)90568-Q
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The crystal structure of phage 434 Cro protein in complex with a 20 base-pair DNA fragment has been determined to 2.5 Å resolution. The DNA fragment contains the sequence of the OR1 operator site. The structure shows a bent conformation for the DNA, straighter at the center and more bent at the ends. The central base-pairs adopt conformations with significant deviations from coplanarity. The two molecules interact extensively along their common interface, both through hydrogen bonds and van der Waals interactions. The significance of these interactions for operator binding and recognition is discussed. © 1991.
引用
收藏
页码:321 / 334
页数:14
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