Home LiteratureArticle Details
PMID: 9096308 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer.

Passner JM, Steitz TA

Abstract

The 2.2 A resolution crystal structure of the Escherichia coli catabolite gene activator protein (CAP) complexed with cAMP and a 46-bp DNA fragment reveals a second cAMP molecule bound to each protein monomer. The second cAMP is in the syn conformation and is located on the DNA binding domain interacting with the helix-turn-helix, a beta-hairpin from the regulatory domain and the DNA (via water molecules). The presence of this second cAMP site resolves the apparent discrepancy between the NMR and x-ray data on the conformation of cAMP, and explains the cAMP concentration-dependent behaviors of the protein. In addition, this site's close proximity to mutations affecting transcriptional activation and its water-mediated interactions with a DNA recognition residue (E181) and DNA raise the possibility that this site has biological relevance.

MeSH Terms
Cyclic AMP/metabolism Cyclic AMP Receptor Protein/metabolism DNA/metabolism DNA-Binding Proteins/metabolism Molecular Sequence Data Molecular Structure Protein Binding
Chemicals
Cyclic AMP Receptor Protein DNA-Binding Proteins DNA Cyclic AMP
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Passner J M
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511, USA.
Steitz T A
References (31)
31 references, click to expand
  1. Conformational transitions of cyclic adenosine monophosphate receptor protein of Escherichia coli. A temperature-jump study.
    Biochemistry. 1974 Jun 4;13(12):2573-8 PMID: 4364837
  2. Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees.
    Science. 1991 Aug 30;253(5023):1001-7 PMID: 1653449
  3. Interaction site of Escherichia coli cyclic AMP receptor protein on DNA of galactose operon promoters.
    Proc Natl Acad Sci U S A. 1979 Oct;76(10):5090-4 PMID: 228278
  4. An equilibrium study of the cooperative binding of adenosine cyclic 3',5'-monophosphate and guanosine cyclic 3',5'-monophosphate to the adenosine cyclic 3',5'-monophosphate receptor protein from Escherichia coli.
    Biochemistry. 1980 Oct 28;19(22):5124-30 PMID: 6257276
  5. Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA.
    Nature. 1981 Apr 30;290(5809):744-9 PMID: 6261152
  6. Conformational selection of syn-cAMP upon binding to the cAMP: receptor protein.
    FEBS Lett. 1981 Dec 21;136(1):160-4 PMID: 6274700
  7. Structure of catabolite gene activator protein at 2.9-A resolution. Incorporation of amino acid sequence and interactions with cyclic AMP.
    J Biol Chem. 1982 Aug 25;257(16):9518-24 PMID: 6286624
  8. Proton nuclear magnetic resonance studies on cyclic nucleotide binding to the Escherichia coli adenosine cyclic 3',5'-phosphate receptor protein.
    Biochemistry. 1982 Aug 17;21(17):4040-8 PMID: 6289868
  9. Autoregulation of the Escherichia coli crp gene: CRP is a transcriptional repressor for its own gene.
    Cell. 1983 Jan;32(1):141-9 PMID: 6297782
  10. Cyclic AMP receptor protein: role in transcription activation.
    Science. 1984 May 25;224(4651):831-8 PMID: 6372090
  11. Mutations that alter the DNA sequence specificity of the catabolite gene activator protein of E. coli.
    Nature. 1984 Sep 20-26;311(5983):232-5 PMID: 6090927
  12. Mutations that alter the allosteric nature of cAMP receptor protein of Escherichia coli.
    EMBO J. 1985 Dec 1;4(12):3329-32 PMID: 3004951
  13. Probing the sequence-specific interaction of the cyclic AMP receptor protein with DNA by site-directed mutagenesis.
    Biochem J. 1987 Mar 15;242(3):645-53 PMID: 3109398
  14. Role of glutamic acid-181 in DNA-sequence recognition by the catabolite gene activator protein (CAP) of Escherichia coli: altered DNA-sequence-recognition properties of [Val181]CAP and [Leu181]CAP.
    Proc Natl Acad Sci U S A. 1987 Sep;84(17):6083-7 PMID: 2888111
  15. Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 A resolution.
    J Mol Biol. 1987 Nov 20;198(2):311-26 PMID: 2828639
  16. Mutations in the cyclic AMP binding site of the cyclic AMP receptor protein of Escherichia coli.
    Biochem J. 1988 Aug 1;253(3):801-7 PMID: 2845936
  17. Escherichia coli cAMP receptor protein: evidence for three protein conformational states with different promoter binding affinities.
    Biochemistry. 1989 Aug 22;28(17):6914-24 PMID: 2554959
  18. Application of fluorescence energy transfer and polarization to monitor Escherichia coli cAMP receptor protein and lac promoter interaction.
    Proc Natl Acad Sci U S A. 1990 Mar;87(5):1744-8 PMID: 2155424
  19. 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.
    Proc Natl Acad Sci U S A. 1990 Jun;87(12):4717-21 PMID: 2162054
  20. Mutations that alter the ability of the Escherichia coli cyclic AMP receptor protein to activate transcription.
    Nucleic Acids Res. 1990 Dec 25;18(24):7243-50 PMID: 2259621
  21. 19F NMR evidence for interactions between the c-AMP binding sites on the c-AMP receptor protein from E. coli.
    FEBS Lett. 1991 May 20;283(1):127-30 PMID: 1645291
  22. The role of two surface exposed loops in transcription activation by the Escherichia coli CRP and FNR proteins.
    Nucleic Acids Res. 1991 Dec 25;19(24):6705-12 PMID: 1762901
  23. Catabolite gene activator protein activation of lac transcription.
    J Bacteriol. 1992 Feb;174(3):655-8 PMID: 1310089
  24. Escherichia coli cyclic AMP receptor protein mutants provide evidence for ligand contacts important in activation.
    J Bacteriol. 1992 Dec;174(24):8030-5 PMID: 1334069
  25. Mutagenesis of the cyclic AMP receptor protein of Escherichia coli: targeting positions 72 and 82 of the cyclic nucleotide binding pocket.
    Nucleic Acids Res. 1993 Apr 25;21(8):1827-35 PMID: 8388097
  26. Mutagenesis of the cyclic AMP receptor protein of Escherichia coli: targeting positions 83, 127 and 128 of the cyclic nucleotide binding pocket.
    Nucleic Acids Res. 1994 Aug 11;22(15):2894-901 PMID: 8065899
  27. Interactions between the Escherichia coli cyclic AMP receptor protein and RNA polymerase at class II promoters.
    Mol Microbiol. 1993 Nov;10(4):789-97 PMID: 7934841
  28. Thermodynamics of cyclic nucleotide binding to the cAMP receptor protein and its T127L mutant.
    J Biol Chem. 1995 Sep 15;270(37):21679-83 PMID: 7665583
  29. Mode of selectivity in cyclic AMP receptor protein-dependent promoters in Escherichia coli.
    Biochemistry. 1996 Jan 30;35(4):1162-72 PMID: 8573570
  30. Orientation of functional activating regions in the Escherichia coli CRP protein during transcription activation at class II promoters.
    Nucleic Acids Res. 1996 Mar 15;24(6):1112-8 PMID: 8604346
  31. Cyclic adenosine 5'-monophosphate in Escherichia coli.
    Bacteriol Rev. 1976 Sep;40(3):527-51 PMID: 186018
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1997-04-01
Pages
2843-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC20284
Subset
IM
Grants
NIGMS NIH HHS · P01 GM022778 · United States
NIGMS NIH HHS · GM22778 · United States
Databases
PDB
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com