Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR.
Eur Biophys J. 2011 Mar;40(3):221-34
Authors: Straus SK, Scott WR, Schwieters CD, Marvin DA
Filamentous bacteriophages (filamentous bacterial viruses or Inovirus) are simple and well-characterised macromolecular assemblies that are widely used in molecular biology and biophysics, both as paradigms for studying basic biological questions and as practical tools in areas as diverse as immunology and solid-state physics. The strains fd, M13 and f1 are virtually identical filamentous phages that infect bacteria expressing F-pili, and are sometimes grouped as the Ff phages. For historical reasons fd has often been used for structural studies, but M13 and f1 are more often used for biological experiments. Many other strains have been identified that are genetically quite distinct from Ff and yet have a similar molecular structure and life cycle. One of these, Pf1, gives the highest resolution X-ray fibre diffraction patterns known for filamentous bacteriophage. These diffraction patterns have been used in the past to derive a molecular model for the structure of the phage. Solid-state NMR experiments have been used in separate studies to derive a significantly different model of Pf1. Here we combine previously published X-ray fibre diffraction data and solid-state NMR data to give a consensus structure model for Pf1 filamentous bacteriophage, and we discuss the implications of this model for assembly of the phage at the bacterial membrane.
Packing Interactions inHydrated and Anhydrous Formsof the Antibiotic Ciprofloxacin: a Solid-State NMR, X-ray Diffraction,and Computer Simulation Study
Packing Interactions inHydrated and Anhydrous Formsof the Antibiotic Ciprofloxacin: a Solid-State NMR, X-ray Diffraction,and Computer Simulation Study
Lui?s Mafra, Se?rgio M. Santos, Rene?e Siegel, Ine?s Alves, Filipe A. Almeida Paz, Dmytro Dudenko and Hans W. Spiess
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Journal of the American Chemical Society
DOI: 10.1021/ja208647n
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Chemical Shifts for the Unusual DNA Structure in Pf1 Bacteriophage from Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR Spectroscopy
Chemical Shifts for the Unusual DNA Structure in Pf1 Bacteriophage from Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR Spectroscopy
Ivan V. Sergeyev, Loren A. Day, Amir Goldbourt and Ann E. McDermott
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Journal of the American Chemical Society
DOI: 10.1021/ja2043062
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Molecular Hydrogen Tweezers: Structure and Mechanisms by Neutron Diffraction, NMR, and Deuterium Labeling Studies in Solid and Solution
Molecular Hydrogen Tweezers: Structure and Mechanisms by Neutron Diffraction, NMR, and Deuterium Labeling Studies in Solid and Solution
Felix Schulz, Victor Sumerin, Sami Heikkinen, Bjo?rn Pedersen, Cong Wang, Michiko Atsumi, Markku Leskela?, Timo Repo, Pekka Pyykko?, Winfried Petry and Bernhard Rieger
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Journal of the American Chemical Society
DOI: 10.1021/ja206394w
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Chemical Shifts for the Unusual DNA Structure in Pf1 Bacteriophage from Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR Spectroscopy.
Chemical Shifts for the Unusual DNA Structure in Pf1 Bacteriophage from Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR Spectroscopy.
Chemical Shifts for the Unusual DNA Structure in Pf1 Bacteriophage from Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR Spectroscopy.
J Am Chem Soc. 2011 Aug 22;
Authors: Sergeyev IV, Day LA, Goldbourt A, McDermott AE
Abstract
Solid state NMR spectra, including dynamic nuclear polarization enhanced 400 MHz spectra acquired at 100K, as well as non-DNP spectra at a variety of field strengths and...
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08-23-2011 04:03 PM
[NMR paper] Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spec
Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy.
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J Mol Biol. 2004 Aug 13;341(3):869-79
Authors: Thiriot DS, Nevzorov AA, Zagyanskiy L, Wu CH, Opella SJ
The atomic resolution structure of Pf1 coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles in solution is compared to the structures previously determined by X-ray fiber and...
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[NMR paper] Structure of the coat protein in fd filamentous bacteriophage particles determined by
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Proc Natl Acad Sci U S A. 2003 May 27;100(11):6458-63
Authors: Zeri AC, Mesleh MF, Nevzorov AA, Opella SJ
The atomic resolution structure of fd coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles differs from that previously determined...
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[NMR paper] Secondary structure of the single-stranded DNA binding protein encoded by filamentous
Secondary structure of the single-stranded DNA binding protein encoded by filamentous phage Pf3 as determined by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Secondary structure of the single-stranded DNA binding protein encoded by filamentous phage Pf3 as determined by NMR.
Eur J Biochem. 1994 Sep 1;224(2):663-76
Authors: Folmer RH, Folkers PJ, Kaan A, Jonker AJ, Aelen JM, Konings RN, Hilbers CW
Nuclear magnetic resonance...
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[NMR paper] On deriving spatial protein structure from NMR or X-ray diffraction data.
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Ciba Found Symp. 1991;161:150-9; discussion 159-66
Authors: van Gunsteren WF, Gros P, Torda AE, Berendsen HJ, van Schaik RC
During the last decade it has become possible to derive the spatial structure of small proteins in solution using multidimensional NMR spectroscopy measurements and interpreting the data in terms of a chemical atomic model. The NMR experiments generate a set...