| Literature DB >> 11804597 |
M D Walkinshaw1, P Taylor, S S Sturrock, C Atanasiu, T Berge, R M Henderson, J M Edwardson, D T F Dryden.
Abstract
We have solved, by X-ray crystallography to a resolution of 1.8 A, the structure of a protein capable of mimicking approximately 20 base pairs of B-form DNA. This ocr protein, encoded by gene 0.3 of bacteriophage T7, mimics the size and shape of a bent DNA molecule and the arrangement of negative charges along the phosphate backbone of B-form DNA. We also demonstrate that ocr is an efficient inhibitor in vivo of all known families of the complex type I DNA restriction enzymes. Using atomic force microscopy, we have also observed that type I enzymes induce a bend in DNA of similar magnitude to the bend in the ocr molecule. This first structure of an antirestriction protein demonstrates the construction of structural mimetics of long segments of B-form DNA.Entities:
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Year: 2002 PMID: 11804597 DOI: 10.1016/s1097-2765(02)00435-5
Source DB: PubMed Journal: Mol Cell ISSN: 1097-2765 Impact factor: 17.970