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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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Journal ArticleDOI

Structure of catabolite gene activator protein at 2.9-A resolution. Incorporation of amino acid sequence and interactions with cyclic AMP.

TL;DR: The amino acid sequence of the Escherichia coli catabolite gene activator protein has been fit into a 2.9-A resolution electron density map and the distribution and nature of side chains in the small domain do not rule out the possibility that catabolites binds to left-handed B-DNA.
Journal ArticleDOI

Cyclic nucleotide-binding domains in proteins having diverse functions.

TL;DR: The overly simplistic view that the protein kinases mediated all of the effects of cAMP and cGMP in eukaryotic tissues has been amended with the discovery of new types of cyclic nucleotide receptors.
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Capturing cyclic nucleotides in action: snapshots from crystallographic studies.

TL;DR: Structural insights have now made it possible to propose a general structural mechanism for how cyclic nucleotides regulate these proteins.
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Nitrogen Assimilation in Escherichia coli: Putting Molecular Data into a Systems Perspective

TL;DR: A comprehensive overview of the hierarchical network of intracellular processes revolving around central nitrogen metabolism in Escherichia coli is presented, with the aim of resolving counterintuitive or paradoxical processes featured in nitrogen assimilation.
Journal ArticleDOI

The cAMP binding domain: An ancient signaling module

TL;DR: It is proposed that the cAMP-binding regulatory proteins function by providing an allosteric system in which the presence or absence of cAMP produces a substantial structural change through the loss of hydrophobic interactions with the adenine ring and consequent repositioning of the C helix.
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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