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Science 30 August 1991:
Vol. 253. no. 5023, pp. 1001 - 1007
DOI: 10.1126/science.1653449
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Articles

Science, Vol 253, Issue 5023, 1001-1007
Copyright © 1991 by American Association for the Advancement of Science

articles

Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees

SC Schultz, GC Shields, and TA Steitz

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.

The 3 angstrom resolution crystal structure of the Escherichia coli catabolite gene activator protein (CAP) complexed with a 30-base pair DNA sequence shows that the DNA is bent by 90 degrees. This bend results almost entirely from two 40 degrees kinks that occur between TG/CA base pairs at positions 5 and 6 on each side of the dyad axis of the complex. DNA sequence discrimination by CAP derives both from sequence-dependent distortion of the DNA helix and from direct hydrogen-bonding interactions between three protein side chains and the exposed edges of three base pairs in the major groove of the DNA. The structure of this transcription factor--DNA complex provides insights into possible mechanisms of transcription activation.


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The Purine Repressor of Bacillus subtilis: a Novel Combination of Domains Adapted for Transcription Regulation.
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Sequence-Dependent Dynamics of Duplex DNA: The Applicability of a Dinucleotide Model.
T. M. Okonogi, S. C. Alley, A. W. Reese, P. B. Hopkins, and B. H. Robinson (2002)
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Transcription Activation by FNR: Evidence for a Functional Activating Region 2.
T. Blake, A. Barnard, S. J. W. Busby, and J. Green (2002)
J. Bacteriol. 184, 5855-5861
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Requirement for two copies of RNA polymerase alpha subunit C-terminal domain for synergistic transcription activation at complex bacterial promoters.
G. S. Lloyd, W. Niu, J. Tebbutt, R. H. Ebright, and S. J.W. Busby (2002)
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Structural Basis of Transcription Activation: The CAP-alpha CTD-DNA Complex.
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D. Lim, K. Poole, and N. C. J. Strynadka (2002)
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Binding sites of different geometries for the 16-3 phage repressor.
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PNAS 99, 8790-8795
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Hidden Markov models from molecular dynamics simulations on DNA.
K. M. Thayer and D. L. Beveridge (2002)
PNAS 99, 8642-8647
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The Escherichia coli Cyclic AMP Receptor Protein Forms a 2:2 Complex with RNA Polymerase Holoenzyme, in Vitro.
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Stoichiometry and Structural Effect of the Cyclic Nucleotide Binding to Cyclic AMP Receptor Protein.
H.-S. Won, T.-W. Lee, S.-H. Park, and B.-J. Lee (2002)
J. Biol. Chem. 277, 11450-11455
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Differential Modulation of DNA Conformation by Estrogen Receptors alpha and beta.
J. R. Schultz, M. A. Loven, V. M. S. Melvin, D. P. Edwards, and A. M. Nardulli (2002)
J. Biol. Chem. 277, 8702-8707
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Identification of Residues in Yeast Spo11p Critical for Meiotic DNA Double-Strand Break Formation.
R. L. Diaz, A. D. Alcid, J. M. Berger, and S. Keeney (2002)
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Structure of Escherichia coli ribosomal protein L25 complexed with a 5S rRNA fragment at 1.8-A resolution.
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Identification and Characterization of a Novel cAMP Receptor Protein in the Cyanobacterium Synechocystis sp. PCC 6803.
H. Yoshimura, T. Hisabori, S. Yanagisawa, and M. Ohmori (2000)
J. Biol. Chem. 275, 6241-6245
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Crystal structure of the human O6-alkylguanine-DNA alkyltransferase.
J. E. A. Wibley, A. E. Pegg, and P. C. E. Moody (2000)
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DNA Distortion Mechanism for Transcriptional Activation by ZntR, a Zn(II)-responsive MerR Homologue in Escherichia coli.
C. E. Outten, F. W. Outten, and T. V. O'Halloran (1999)
J. Biol. Chem. 274, 37517-37524
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The cAMP receptor protein CRP can function as an osmoregulator of transcription in Escherichia coli.
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Interaction of calicheamicin gamma 1I and its related carbohydrates with DNA-protein complexes.
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B. W. Allan, R. Garcia, K. Maegley, J. Mort, D. Wong, W. Lindstrom, J. M. Beechem, and N. O. Reich (1999)
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Crystal Structure of the Z Domain of the Human Editing Enzyme ADAR1 Bound to Left-Handed Z-DNA.
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