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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Journal ArticleDOI
SPKK, a new nucleic acid-binding unit of protein found in histone.
TL;DR: A new DNA‐binding unit of a protein different from the alpha‐helix, the beta‐sheet and the Zn‐finger is proposed based on the analysis of the structure of the N‐terminus of sea urchin spermatogenous histone H1.
Journal ArticleDOI
Mutations that alter the DNA sequence specificity of the catabolite gene activator protein of E. coli
TL;DR: It is proposed that it is this amino acid of CAP that makes contacts with base pairs 7 and 16 of the symmetrical recognition site of the catabolite gene activator protein.
Journal ArticleDOI
Mechanism of CRP-cAMP activation of lac operon transcription initiation activation of the P1 promoter☆
TL;DR: DNA supercoiling enhanced the promoter strength of the lac wild-type and UV5 promoters and CRP-cAMP was necessary for optimal promoter strength for the lacWild-type promoter.
Book ChapterDOI
Cyclic nucleotide gated channels.
Martin Biel,Stylianos Michalakis +1 more
TL;DR: In this paper, the authors give an overview on the molecular properties of cyclic nucleotide-gated (CNG) channels and describe the signal transduction pathways these channels are involved in.
Journal ArticleDOI
Homology between CAP and Fnr, a regulator of anaerobic respiration in Escherichia coli
TL;DR: Three regions of sequence homology suggest that Fnr and CAP may have similar three-dimensional structures and that the regulation of anaerobic energy metabolism may involve interaction between FnR and an unidentified effector molecule.
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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