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

JOURNAL OF MOLECULAR BIOLOGY

卷:286

Article

Tan, WM ; Jelinek, R ; Opella, SJ ; Malik, P ; Terry, TD ; Perham, RN

关键词: filamentous bacteriophage;    fd;    major coat protein;    pVIII;    solid-state NMR spectroscopy;   

DOI  :  10.1006/jmbi.1998.2517

来源: Elsevier

【 摘 要 】

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. (C) 1999 Academic Press.

【 授权许可】

Free