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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Mutagenesis of the cysteine residues in the transcription factor NtcA from Anabaena PCC 7120 and its effects on DNA binding in vitro.
TL;DR: The experiments show that the DNA binding in vitro is stronger in the presence of the reducing agent DTT than in its absence, and this effect is not due to breaking of a disulfide bond between the cysteine residues, since the double mutant containing no cysteines was also affected by DTT.
Journal ArticleDOI
Purification of ArcR, an oxidation-sensitive regulatory protein from Bacillus licheniformis.
TL;DR: Alkylation of mutant proteins with single substitutions showed that both cysteine residues of the protein, C178 and C205, are involved in formation of the disulfide bridges and yielded a functional protein insensitive to oxidation and able to form a complex with its cognate target on the DNA.
Journal ArticleDOI
Allosteric control of promoter DNA bending by cyclic AMP receptor and cyclic AMP.
TL;DR: The cyclic AMP receptor-promoter complex is driven into its specific bent form in vitro in the range of cAMP concentrations corresponding to that required for gene regulation in vivo.
Journal ArticleDOI
Protein-induced DNA linking number change by sequence-specific DNA binding proteins and its biological effects
TL;DR: It was shown recently that LacI utilizes the constrained superhelicity (ΔLk) in LacI-lac O1 complexes and serves as a topological barrier to constrain free, unconstrained (−) supercoils within the 401-bp DNA loop.
Journal ArticleDOI
Generation of deletions in the 3'-flanking sequences of the Escherichia coli crp gene that induce cyclic AMP suppressor functions.
J W Barton,T Melton +1 more
TL;DR: The delta crp-4 mutation demonstrates that sequences distal to the crp structural gene can mediate cyclic AMP suppressor functions.
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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