From 'I' to 'L' and back again: the odyssey of membrane-bound M13 protein.
The major coat protein of the filamentous bacteriophage M13 is a surprising protein because it exists both as a membrane protein and as part of the M13 phage coat during its life cycle. Early studies showed that the phage-bound structure of the coat protein was a continuous I-shaped alpha-helix. However, throughout the years various structural models, both I-shaped and L-shaped, have been proposed for the membrane-bound state of the coat protein. Recently, site-directed labelling approaches have enabled the study of the coat protein under conditions that more closely mimic the in vivo membrane-bound state. Interestingly, the structure that has emerged from this work is I-shaped and similar to the structure in the phage-bound state.
Vos
Werner L
WL
Department of Biology, National University of Ireland Maynooth, County Kildare, Ireland.
Nazarov
Petr V
PV
Koehorst
Rob B M
RB
Spruijt
Ruud B
RB
Hemminga
Marcus A
MA
D000595:Amino Acid Sequence; D017104:Bacteriophage M13 / Q000378:metabolism*; D036022:Capsid Proteins / Q000737:chemistry* / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D008954:Models, Biological; D008969:Molecular Sequence Data; D011487:Protein Conformation
D036022:Capsid Proteins; D008565:Membrane Proteins