Literature DB >> 2834718

Electrostatic calculations and model-building suggest that DNA bound to CAP is sharply bent.

J Warwicker1, B P Engelman, T A Steitz.   

Abstract

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 potential field of CAP shows regions of positive potential that form 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.

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Year:  1987        PMID: 2834718     DOI: 10.1002/prot.340020404

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  26 in total

1.  Modeling helix-turn-helix protein-induced DNA bending with knowledge-based distance restraints.

Authors:  W S Tzou; M J Hwang
Journal:  Biophys J       Date:  1999-09       Impact factor: 4.033

2.  Simplified methods for pKa and acid pH-dependent stability estimation in proteins: removing dielectric and counterion boundaries.

Authors:  J Warwicker
Journal:  Protein Sci       Date:  1999-02       Impact factor: 6.725

3.  Induced fit and the entropy of structural adaptation in the complexation of CAP and lambda-repressor with cognate DNA sequences.

Authors:  Surjit B Dixit; David Q Andrews; D L Beveridge
Journal:  Biophys J       Date:  2005-02-24       Impact factor: 4.033

4.  Escherichia coli catabolite gene activator protein mutants defective in positive control of lac operon transcription.

Authors:  A C Eschenlauer; W S Reznikoff
Journal:  J Bacteriol       Date:  1991-08       Impact factor: 3.490

5.  Bending of synthetic bacteriophage 434 operators by bacteriophage 434 proteins.

Authors:  G B Koudelka
Journal:  Nucleic Acids Res       Date:  1991-08-11       Impact factor: 16.971

Review 6.  Structural aspects of protein-DNA recognition.

Authors:  P S Freemont; A N Lane; M R Sanderson
Journal:  Biochem J       Date:  1991-08-15       Impact factor: 3.857

7.  Identification of a contact between arginine-180 of the catabolite gene activator protein (CAP) and base pair 5 of the DNA site in the CAP-DNA complex.

Authors:  X P Zhang; R H Ebright
Journal:  Proc Natl Acad Sci U S A       Date:  1990-06       Impact factor: 11.205

8.  Consensus DNA site for the Escherichia coli catabolite gene activator protein (CAP): CAP exhibits a 450-fold higher affinity for the consensus DNA site than for the E. coli lac DNA site.

Authors:  R H Ebright; Y W Ebright; A Gunasekera
Journal:  Nucleic Acids Res       Date:  1989-12-25       Impact factor: 16.971

9.  Sequence-dependent contribution of distal binding domains to CAP protein-DNA binding affinity.

Authors:  D D Dalma-Weiszhausz; M R Gartenberg; D M Crothers
Journal:  Nucleic Acids Res       Date:  1991-02-11       Impact factor: 16.971

10.  Ribosomal protein L7/L12 has a helix-turn-helix motif similar to that found in DNA-binding regulatory proteins.

Authors:  P A Rice; T A Steitz
Journal:  Nucleic Acids Res       Date:  1989-05-25       Impact factor: 16.971

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