Literature DB >> 21082179

Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR.

S K Straus1, W R P Scott, C D Schwieters, D A Marvin.   

Abstract

Filamentous bacteriophages (n class="Disease">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.

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Year:  2010        PMID: 21082179      PMCID: PMC5545983          DOI: 10.1007/s00249-010-0640-9

Source DB:  PubMed          Journal:  Eur Biophys J        ISSN: 0175-7571            Impact factor:   1.733


  52 in total

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2.  On the structures of filamentous bacteriophage Ff (fd, f1, M13).

Authors:  S K Straus; W R P Scott; M F Symmons; D A Marvin
Journal:  Eur Biophys J       Date:  2007-10-18       Impact factor: 1.733

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Journal:  J Biomol NMR       Date:  2002-03       Impact factor: 2.835

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7.  Macromolecular structural transitions in Pf1 filamentous bacterial virus.

Authors:  C Nave; A G Fowler; S Malsey; D A Marvin; H Siegrist; E J Wachtel
Journal:  Nature       Date:  1979-09-20       Impact factor: 49.962

8.  Phage-induced alignment of membrane proteins enables the measurement and structural analysis of residual dipolar couplings with dipolar waves and lambda-maps.

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Journal:  J Am Chem Soc       Date:  2009-10-14       Impact factor: 15.419

9.  Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy.

Authors:  David S Thiriot; Alexander A Nevzorov; Lena Zagyanskiy; Chin H Wu; Stanley J Opella
Journal:  J Mol Biol       Date:  2004-08-13       Impact factor: 5.469

10.  Hydrogen bonding in high-resolution protein structures: a new method to assess NMR protein geometry.

Authors:  Rebecca S Lipsitz; Yugal Sharma; Bernard R Brooks; Nico Tjandra
Journal:  J Am Chem Soc       Date:  2002-09-04       Impact factor: 15.419

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  7 in total

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3.  Xplor-NIH for molecular structure determination from NMR and other data sources.

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Review 4.  Three-dimensional reconstruction of helical polymers.

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Review 6.  Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins.

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Review 7.  Pf Bacteriophage and Their Impact on Pseudomonas Virulence, Mammalian Immunity, and Chronic Infections.

Authors:  Patrick R Secor; Elizabeth B Burgener; M Kinnersley; Laura K Jennings; Valery Roman-Cruz; Medeea Popescu; Jonas D Van Belleghem; Naomi Haddock; Conner Copeland; Lia A Michaels; Christiaan R de Vries; Qingquan Chen; Julie Pourtois; Travis J Wheeler; Carlos E Milla; Paul L Bollyky
Journal:  Front Immunol       Date:  2020-02-21       Impact factor: 7.561

  7 in total

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