Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 321-334 |
| Number of pages | 14 |
| Journal | Journal of Molecular Biology |
| Volume | 219 |
| Issue number | 2 |
| DOIs | |
| State | Published - May 20 1991 |
Funding
We thank Marie Drottar for her essential role in crystallization and purificat,ion of protein and D?u’A. \Vr t,hank M. Ptashnr for continued int,rrest and collabo-rat,ion. and A. hggarwal. M. Hlum. (:. Koudelka. I). Rodgers, and C!. Wolberger for help and suggestions. This work was supported by NIH grant, GM-29109 (to M. Ptashne). A.M. was a post-doctoral fellow of the I)amon Runyon-Walt’er WinchelI Cancer Researclh Fund (DRC: 878).
Keywords
- DNA conformation
- DNA recognition
- X-ray crystallography
- helix-turn-helix
- repressor
ASJC Scopus subject areas
- Molecular Biology
- Structural Biology