NMR Studies of the Structure and Dynamics of Membrane-Bound Bacteriophage Pf1 Coat Protein

Filamentous bacteriophage coat protein undergoes a remarkable structural transition during the viral assembly process as it is transferred from the membrane environment of the cell, where it spans the phospholipid bilayer, to the newly extruded virus particles. Nuclear magnetic resonance (NMR) studi...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1991-05, Vol.252 (5010), p.1303-1305
Main Authors: Shon, Ki-Joon, Kim, Yongae, Colnago, Luiz A., Opella, Stanley J.
Format: Article
Language:English
Subjects:
Amides
Bacteriophages
Biochemistry
Capsid - chemistry
Capsid - metabolism
Capsid Proteins
Cell Membrane - metabolism
Lipid Bilayers - metabolism
Magnetic fields
Magnetic Resonance Spectroscopy
Membrane proteins
Micelles
Models, Molecular
Molecular Structure
Nuclear magnetic resonance
Nuclear magnetic resonance spectroscopy
Phospholipids
Protein Conformation
Proteins
Resonance
Spectroscopy
Viral morphology
Virions
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Summary:Filamentous bacteriophage coat protein undergoes a remarkable structural transition during the viral assembly process as it is transferred from the membrane environment of the cell, where it spans the phospholipid bilayer, to the newly extruded virus particles. Nuclear magnetic resonance (NMR) studies show the membrane-bound form of the 46-residue Pf1 coat protein to be surprisingly complex with five distinct regions. The secondary structure consists of a long hydrophobic helix (residues 19 to 42) that spans the bilayer and a short amphipathic helix (residues 6 to 13) parallel to the plane of the bilayer. The NH$_2$-terminus (residues 1 to 5), the COOH-terminus (residues 43 to 46), and residues 14 to 18 connecting the two helices are mobile. By comparing the structure and dynamics of the membrane-bound coat protein with that of the viral form as determined by NMR and neutron diffraction, essential features of assembly process can be identified.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1925542