Effects of temperature and Y21M mutation on conformational heterogeneity of the major coat protein (pVIII) of filamentous bacteriophage fd

Wee M. Tan, Raz Jelinek, Stanley J. Opella, Pratap Malik, Tamsin D. Terry, Richard N. Perham

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

Abstract

Solid-state NMR spectroscopy was used to analyze the conformational heterogeneity of the major coat protein (pVIII) of filamentous bacteriophage fd. Both one and two-dimensional solid-state NMR spectra of magnetically aligned samples of fd bacteriophage reveal that an increase in temperature and a single site substitution (Tyr21 to Met, Y21M) reduce the conformational heterogeneity observed throughout wild-type pVIII. The NMR results are consistent with previous studies indicating that conformational flexibility in the hinge-bend segment that links the amphipathic and hydrophobic helices in the membrane-bound form of the protein plays an essential role during phage assembly, which involves a major change in the tertiary, but not secondary, structure of the coat protein.

Original languageEnglish
Pages (from-to)787-796
Number of pages10
JournalJournal of Molecular Biology
Volume286
Issue number3
DOIs
StatePublished - 26 Feb 1999
Externally publishedYes

Keywords

  • Filamentous bacteriophage
  • Major coat protein
  • Solid-state NMR spectroscopy
  • fd
  • pVIII

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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