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PMID: 2038059 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The phage 434 Cro/OR1 complex at 2.5 A resolution.

Journal of molecular biology ·Vol. 219 ·No. 2 ·1991-05-20 ·Pages 321-34

Mondragón A, Harrison SC

Abstract

The crystal structure of phage 434 Cro protein in complex with a 20 base-pair DNA fragment has been determined to 2.5 A 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.

MeSH Terms
Amino Acid Sequence Bacteriophages/analysis,genetics Base Composition Base Sequence DNA, Viral/chemistry,metabolism DNA-Binding Proteins Genes, Viral Models, Molecular Molecular Sequence Data Nucleic Acid Conformation Protein Conformation Repressor Proteins/chemistry,isolation & purification,metabolism Viral Proteins Viral Regulatory and Accessory Proteins X-Ray Diffraction/methods
Chemicals
DNA, Viral DNA-Binding Proteins Repressor Proteins Viral Proteins Viral Regulatory and Accessory Proteins phage repressor proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Mondragón A
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.
Harrison S C
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
Published
1991-05-20
Pages
321-34
Language
English
Region
England
NLM ID
2985088R
Subset
IM
Grants
NIGMS NIH HHS · GM-29109 · United States
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