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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Requirement of the avian retrovirus pp32 DNA binding protein domain for replication.
TL;DR: The NH2-terminal amino acid sequence of the pp32 DNA binding protein has been determined, thus establishing its precise coding region in the polymerase gene of Rous sarcoma virus.
Journal ArticleDOI
Ribosomal protein S7: a new RNA-binding motif with structural similarities to a DNA architectural factor.
Harumi Hosaka,Atsushi Nakagawa,Isao Tanaka,Nao Harada,Kazunari Sano,Makoto Kimura,Min Yao,Soichi Wakatsuki +7 more
TL;DR: The molecular structure of S7, together with the results of previous cross-linking experiments, suggest how this ribosomal protein binds to the 3' major domain of 16S rRNA and mediates the folding of 16s rRNA to create the ribosome decoding centre.
Journal ArticleDOI
The transcription factor DNR from Pseudomonas aeruginosa specifically requires nitric oxide and haem for the activation of a target promoter in Escherichia coli.
TL;DR: It is shown, for the first time, that DNR is able to discriminate in vivo between different diatomic signal molecules, NO and CO, both ligands of the reduced haem iron in vitro, suggesting that D NR responds specifically to NO.
Journal ArticleDOI
Fast and Slow Cyclic Nucleotide-dissociation Sites in cAMP-dependent Protein Kinase Are Transposed in Type Iβ cGMP-dependent Protein Kinase
Robin B. Reed,Mårten Sandberg,Tore Jahnsen,Suzanne M. Lohmann,Sharron H. Francis,Jackie D. Corbin +5 more
TL;DR: In type Iβ cGK, the slow cGMP-binding site is identified as the amino-terminal site in contrast to the order assigned to the fast and slow cAMP-binding sites of cAK, thus establishing the importance of the hydroxyl group of Thr-193 and −317 for cG MP binding to c GK.
Journal ArticleDOI
Crystal structure of the factor for inversion stimulation FIS at 2.0 A resolution.
TL;DR: The factor for inversion stimulation (FIS) binds as a homodimeric molecule to a loose 15 nucleotide consensus sequence in DNA, which stimulates DNA-related processes, such as DNA inversion and excision, it activates transcription of tRNA and rRNA genes and it regulates its own synthesis.
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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