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Title: From 'I' to 'L' and back again: the odyssey of membrane-bound M13 protein. Author: Vos WL, Nazarov PV, Koehorst RB, Spruijt RB, Hemminga MA. Journal: Trends Biochem Sci; 2009 May; 34(5):249-55. PubMed ID: 19362002. 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 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.[Abstract] [Full Text] [Related] [New Search]