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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Recognition of promoter DNA by subdomain 4.2 of Escherichia coli sigma 70: a knowledge based model of -35 hexamer interaction with 4.2 helix-turn-helix motif
TL;DR: In Escherichia coli, subdomains 2.4 and 4.2 of the primary transcription factor sigma 70 are the most highly conserved regions and are responsible for the recognition of -10 and -35 promoter elements respectively, suggesting that sigma factor also belongs to the HTH class of proteins.
Journal ArticleDOI
A novel role for Crp in controlling magnetosome biosynthesis in Magnetospirillum gryphiswaldense MSR-1
TL;DR: This is the first time to demonstrate that Crp plays an important role in controlling magnetosome biomineralization and provides reliable expression profile data that elucidate the mechanism of Crp regulation of magnetosomes formation in MSR-1.
Journal ArticleDOI
PHOTOCHEMICAL CROSS‐LINKING OF THE CYCLIC ADENOSINE 3′, 5′MONOPHOSPHATE RECEPTOR PROTEIN TO Escherichia coli 5‐BROMOURACIL‐SUBSTITUTED DNA. ROLE OF THE EFFECTORS
TL;DR: Results show that the protein in the CRP‐cGMP complex behaves differently from the free protein, and it is shown that tryptophyl residues are more photoreactive than tyrosyl ones.
Journal ArticleDOI
Crystal structure of adenine-1-(2-carboxyethyl)uracil (1:1) complex: a model for interactions of amino acid side chains with nucleic acid base pair
TL;DR: In this article, the title complex of the protein-nucleic acid interactions was determined by X-ray analysis, and the space group is P21/c with the unit cell dimensions of a=12.567(1), b=13.358(1, c=8.032(1) A and β=93.28°.
Journal ArticleDOI
Conformational microheterogeniety in a DNA double helix: Structure of restriction endonuclease Bam H1 recognition site
TL;DR: It is demonstrated that conformational microheterogeneity with a structural two fold, is present in the Bam H1 recognition site.
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
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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
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Journal ArticleDOI
Three-Dimensional Structure of Immunoglobulins
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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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