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
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A proton nuclear magnetic resonance and nuclear overhauser effect (NOE) study of human plasma prealbumin, including the development and application to spectral assignment of a combined ring current shift and NOE prediction program.
David G. Reid,M R Saunders +1 more
TL;DR: Assignment of a number of residues was aided by the development of a computer program, PARSNIP (Programme to Analyse Ring current Shifts and nuclear Overhauser effects in Proteins), which employs high resolution x-ray crystal structure atomic co-ordinates to calculate structure-dependent ring current-induced shifts of aromatic and methyl group protons.
Journal ArticleDOI
A chimeric activator of transcription that uses two DNA-binding domains to make simultaneous contact with pairs of recognition sites
TL;DR: The results show how such a bivalent DNA‐binding protein can be used to regulate transcription differentially from promoters that bear either one or both recognition sites.
Journal ArticleDOI
Crystallization of and preliminary X-ray diffraction data for TET-repressor and the TET-repressor-tetracycline complex
TL;DR: The TET-repressor encoded by the transposon Tn10 has been crystallized along with the repressor-tetracycline complex, suggesting that only minor, subtle changes in structure trigger binding to or release of the operator.
Journal ArticleDOI
Conservation and divergence of Grb7 family of Ras-binding domains.
TL;DR: The results suggest that Grb14 might have been evolved later in the evolution that binds to both Ras and nucleotide binding proteins such as CNGA1 and eukaryotic CNG channels could be evolved through a gene fusion between prokaryotic ion channels and cyclic nucleotidebinding proteins.
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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