Literature DB >> 18421454

The hand of the filamentous bacteriophage helix.

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

Abstract

Filamentous bacteriophage (Inovirus) is a widely studied model system in molecular biophysics. The structure of the virion has been analysed by various methods, but the methods have seldom questioned the hand of the virion helix. The hand of the helix relating the protein subunits in the class II virus strain Pf1 was chosen by calculating an electron-density distribution from X-ray fibre diffraction data, using a maximum-entropy method, but to our knowledge this method has not been used for a similar purpose in any other system. Moreover, this same hand was extended only by analogy, with no direct analysis of the corresponding data, to the class I virus strain Ff (fd, f1, M13), which has a different helix symmetry. Here we use published solid-state NMR data to confirm the validity of the hand of Pf1 chosen by the maximum-entropy method, and to confirm the extension to Ff.

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Year:  2008        PMID: 18421454     DOI: 10.1007/s00249-008-0327-7

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


  24 in total

1.  Imaging membrane protein helical wheels.

Authors:  J Wang; J Denny; C Tian; S Kim; Y Mo; F Kovacs; Z Song; K Nishimura; Z Gan; R Fu; J R Quine; T A Cross
Journal:  J Magn Reson       Date:  2000-05       Impact factor: 2.229

2.  The molecular structure and structural transition of the alpha-helical capsid in filamentous bacteriophage Pf1.

Authors:  L C Welsh; M F Symmons; D A Marvin
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2000-02

3.  The Xplor-NIH NMR molecular structure determination package.

Authors:  Charles D Schwieters; John J Kuszewski; Nico Tjandra; G Marius Clore
Journal:  J Magn Reson       Date:  2003-01       Impact factor: 2.229

4.  Using pisa pies to resolve ambiguities in angular constraints from PISEMA spectra of aligned proteins.

Authors:  Francesca M Marassi; Stanley J Opella
Journal:  J Biomol NMR       Date:  2002-07       Impact factor: 2.835

5.  Molecular structure of fd (f1, M13) filamentous bacteriophage refined with respect to X-ray fibre diffraction and solid-state NMR data supports specific models of phage assembly at the bacterial membrane.

Authors:  D A Marvin; L C Welsh; M F Symmons; W R P Scott; S K Straus
Journal:  J Mol Biol       Date:  2005-11-08       Impact factor: 5.469

6.  Pf1 Inovirus. Electron density distribution calculated by a maximum entropy algorithm from native fibre diffraction data to 3 A resolution and single isomorphous replacement data to 5 A resolution.

Authors:  D A Marvin; R K Bryan; C Nave
Journal:  J Mol Biol       Date:  1987-01-20       Impact factor: 5.469

7.  Molecular dynamics in refinement against fiber diffraction data.

Authors:  H Wang; G Stubbs
Journal:  Acta Crystallogr A       Date:  1993-05-01       Impact factor: 2.290

8.  Structure and assembly of filamentous bacterial viruses.

Authors:  D A Marvin; E J Wachtel
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  1976-11-30       Impact factor: 6.237

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

Authors:  Ana Carolina Zeri; Michael F Mesleh; Alexander A Nevzorov; Stanley J Opella
Journal:  Proc Natl Acad Sci U S A       Date:  2003-05-15       Impact factor: 11.205

10.  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

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  1 in total

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

Authors:  S K Straus; W R P Scott; C D Schwieters; D A Marvin
Journal:  Eur Biophys J       Date:  2010-11-17       Impact factor: 1.733

  1 in total

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