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Electrostatic calculations and model‐building suggest that DNA bound to CAP is sharply bent
Author(s) -
Warwicker J.,
Engelman B.P.,
Steitz T.A.
Publication year - 1987
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340020404
Subject(s) - dna , bent molecular geometry , operon , electrostatics , activator (genetics) , affinities , chemistry , crystallography , gene , biophysics , physics , biology , stereochemistry , escherichia coli , biochemistry , organic chemistry
Two observations suggest that DNA, upon binding to E. coli catabolite gene activator protein (CAP), is sharply bent by a total angle of at least 100–150 degrees: (1) The electrostatic protential field of CAP shows regions of positive potential that from a ramp on 3 sides of the protein. (2) The DNA binding site size as determined by DNA ethylation interference with binding, (Majors: “ Control of the E. coli Lac Operon at the Molecular Level. ” Ph.D. Thesis, Harvard University, Cambridge, 1977) and by relative affinities of DNA fragments of various lengths (Liu‐Johnson et al.: Cell 47:995–1005, 1986) requires severe bending of the DNA to maintain its favorable electrostatic contact with the protein.