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Journal ArticleDOI

Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA

David B. McKay, +1 more
- 30 Apr 1981 - 
- Vol. 290, Iss: 5809, pp 744-749
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.

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Citations
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Structure of a transporter domain emerges

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Cyclic Nucleotide-Gated Channels: Classification, Structure and Function, Activators and Inhibitors

TL;DR: Cyclic nucleotide-gated channels are ion channels the gating of which is directly controlled by cyclic nucleotides, and play crucial roles in visual and olfactory transductions.
Journal ArticleDOI

Allosteric Response of DNA Recognition Helices of Catabolite Activator Protein to cAMP and DNA Binding

TL;DR: The revelation that the predicted allosteric pathways crisscross the inter subunit interface offers important clues on the microscopic origin of the intersubunit cooperativity and dimer stability of CAP.
DissertationDOI

Coil 2 of intermediate filaments: its complete structure and impact of desminopathy-related mutations.

TL;DR: The dimer structure of vimentin was further investigated using a ‘divide-and-conquer’ approach and it is shown that all fragments were [alpha]-helical, a conserved structural feature to all IF proteins.
Proceedings ArticleDOI

3-D display for molecular structure by using a moving mirror

TL;DR: In this paper, the authors devised a 3D display with a linearly moving mirror to reflect a series of 2-D cross sections of the 3-D image on a CRT.
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

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

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.

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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