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  • 1
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    Structural basis of transcription activation: the CAP-alpha CTD-DNA complex (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-31
    Description: The Escherichia coli catabolite activator protein (CAP) activates transcription at P(lac), P(gal), and other promoters through interactions with the RNA polymerase alpha subunit carboxyl-terminal domain (alphaCTD). We determined the crystal structure of the CAP-alphaCTD-DNA complex at a resolution of 3.1 angstroms. CAP makes direct protein-protein interactions with alphaCTD, and alphaCTD makes direct protein-DNA interactions with the DNA segment adjacent to the DNA site for CAP. There are no large-scale conformational changes in CAP and alphaCTD, and the interface between CAP and alphaCTD is small. These findings are consistent with the proposal that activation involves a simple "recruitment" mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benoff, Brian -- Yang, Huanwang -- Lawson, Catherine L -- Parkinson, Gary -- Liu, Jinsong -- Blatter, Erich -- Ebright, Yon W -- Berman, Helen M -- Ebright, Richard H -- GM21589/GM/NIGMS NIH HHS/ -- GM41376/GM/NIGMS NIH HHS/ -- GM64375/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 30;297(5586):1562-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Waksman Institute and Department of Chemistry, Howard Hughes Medical Institute, Rutgers University, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12202833" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography, X-Ray ; Cyclic AMP Receptor Protein/*chemistry/metabolism/physiology ; DNA/*chemistry/metabolism ; DNA-Directed RNA Polymerases/*chemistry/metabolism/physiology ; Macromolecular Substances ; Models, Molecular ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; Structure-Activity Relationship ; *Transcription, Genetic ; Transcriptional Activation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-07
    Description: The structure of a protein triple helix has been determined at 1.9 angstrom resolution by x-ray crystallographic studies of a collagen-like peptide containing a single substitution of the consensus sequence. This peptide adopts a triple-helical structure that confirms the basic features determined from fiber diffraction studies on collagen: supercoiling of polyproline II helices and interchain hydrogen bonding that follows the model II of Rich and Crick. In addition, the structure provides new information concerning the nature of this protein fold. Each triple helix is surrounded by a cylinder of hydration, with an extensive hydrogen bonding network between water molecules and peptide acceptor groups. Hydroxyproline residues have a critical role in this water network. The interaxial spacing of triple helices in the crystal is similar to that in collagen fibrils, and the water networks linking adjacent triple helices in the crystal structure are likely to be present in connective tissues. The breaking of the repeating (X-Y-Gly)n pattern by a Gly--〉Ala substitution results in a subtle alteration of the conformation, with a local untwisting of the triple helix. At the substitution site, direct interchain hydrogen bonds are replaced with interstitial water bridges between the peptide groups. Similar conformational changes may occur in Gly--〉X mutated collagens responsible for the diseases osteogenesis imperfecta, chondrodysplasias, and Ehlers-Danlos syndrome IV.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bella, J -- Eaton, M -- Brodsky, B -- Berman, H M -- AR 19626/AR/NIAMS NIH HHS/ -- GM 21589/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):75-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Rutgers University, New Brunswick, NJ 08855.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7695699" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/chemistry ; Amino Acid Sequence ; Collagen/*chemistry ; Computer Graphics ; Crystallography, X-Ray ; Glycine/chemistry ; Hydrogen Bonding ; Hydroxyproline/chemistry ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Peptides/*chemistry ; *Protein Conformation ; Protein Structure, Secondary
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    How Eco RI recognizes and cuts DNA (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-12-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berman, H M -- New York, N.Y. -- Science. 1986 Dec 19;234(4783):1482-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3024319" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallization ; Crystallography ; DNA/*metabolism ; DNA Restriction Enzymes/*metabolism ; Deoxyribonuclease EcoRI ; Nucleic Acid Conformation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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