Journal ArticleDOI
Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA
David B. McKay,Thomas A. Steitz +1 more
TLDR
The 2.9 Å resolution crystal structure of Escherichia coli catabolite gene activator protein (CAP) completed with cyclic AMP reveals two distinct structural domains separated by a cleft, suggesting that the CAP conversion of right- to left-handed DNA in a closed supercoil, is what activates transcription by RNA polymerase.Abstract:
The 2.9 A resolution crystal structure of Escherichia coli catabolite gene activator protein (CAP) complexed with cyclic AMP reveals two distinct structural domains separated by a cleft. The smaller carboxy-terminal domain is presumed to bind DNA while the amino-terminal domain is seen to bind cyclic AMP. Model building studies suggest that CAP binds to left-handed B-type DNA, contracting its major groove via two alpha-helices. It is possible that the CAP conversion of right- to left-handed DNA in a closed supercoil, is what activates transcription by RNA polymerase.read more
Citations
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Journal ArticleDOI
Structural snapshot of cyclic nucleotide binding domains from cyclic nucleotide-sensitive ion channels.
Sven Schünke,Matthias Stoldt +1 more
TL;DR: Structural insights about cyclic nucleotide-binding-induced conformational changes in CNBDs are described and their potential coupling with channel gating is described.
Journal ArticleDOI
1H NMR study of the interaction of bacteriophage lambda Cro protein with the OR3 operator. II. Assignment of the non-exchangeable proton resonances of the OR3 operator.
Klaus-Dieter Hahn,Friedrich Buck,Heinz Rüterjans,B.K. Chernov,Konstantin G. Skryabin,Kirpichnikov Mp +5 more
TL;DR: In this paper, the 17 base pair operator OR3 oligonucleotide, which is the preferential binding site for the Cro repressor of phage λ, was studied by two-dimensional NMR spectroscopy.
Journal ArticleDOI
X-ray diffraction analysis of crystals of bovine platelet factor 4.
TL;DR: Bovine platelet factor 4 has been crystallized by "vapor dilution" in space group P2( 1)2(1)2 (1) 2(1), a = 63.7 A, b = 66.5 A, with four molecules in the asymmetric unit.
Journal ArticleDOI
UV oxidation of cyclic AMP receptor protein, a global bacterial gene regulator, decreases DNA binding and cleaves DNA at specific sites
Fabian Leinisch,Michele Mariotti,Sofie Hagel Andersen,Søren Lindemose,Per Hägglund,Niels Erik Møllegaard,Michael J. Davies +6 more
TL;DR: Modification to CRP, and bound DNA, contributes to UV sensitivity, and the modifications at the CRP dimer interface are proposed to occur via oxidation of two species Met residues to reactive persulfoxides that damage neighbouring amino acids and DNA bases.
References
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Journal ArticleDOI
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution.
TL;DR: The haemagglutinin glycoprotein of influenza virus is a trimer comprising two structurally distinct regions: a triple-stranded coiled-coil of α-helices extends 76 Å from the membrane and a globular region of antiparallel β-sheet is positioned on top of this stem.
Journal ArticleDOI
Molecular structure of a left-handed double helical DNA fragment at atomic resolution
Andrew H.-J. Wang,Gary J. Quigley,F. Kolpak,J.L. Crawford,J. H. Van Boom,G. A. Van Der Marel,Alexander Rich +6 more
TL;DR: The DNA fragment d(CpGpCpC pGp CpG pG) crystallises as a left-handed double helical molecule with Watson–Crick base pairs and an antiparallel organisation of the sugar phosphate chains.
Journal ArticleDOI
Optimised parameters for A-DNA and B-DNA
TL;DR: The molecular structures presented have the most probable values of bond-lengths, bond-angles and furanose ring conformations as defined by accurate X-ray crystallographic analyses of relevant monomers.
Journal ArticleDOI
Three-Dimensional Structure of Immunoglobulins
L M Amzel,Roberto J. Poljak +1 more
TL;DR: This chapter discusses a study analyzing the three-dimensional structure of immunoglobulins, in which the periodicity of the crystal was used to reduce the background noise and reveal the molecular outline.
Journal ArticleDOI
Tomato bushy stunt virus at 2.9 A resolution.
Stephen C. Harrison,Arthur J. Olson,Clarence E. Schutt,Clarence E. Schutt,Frank Winkler,Frank Winkler,Gérard Bricogne +6 more
TL;DR: The polypeptide chain of a TBSV subunit folds into two domains, connected by a hinge, and a flexibly-linked N-terminal arm, and RNA is also not uniquely fixed to sites on the major domains.
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