Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2031280 | Trends in Biochemical Sciences | 2009 | 7 Pages |
Abstract
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 α-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.
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Authors
Werner L. Vos, Petr V. Nazarov, Rob B.M. Koehorst, Ruud B. Spruijt, Marcus A. Hemminga,