From 'I' to 'L' and back again: the odyssey of membrane-bound M13 protein

Werner L. Vos*, Petr V. Nazarov, Rob B.M. Koehorst, Ruud B. Spruijt, Marcus A. Hemminga

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

16 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)249-255
Number of pages7
JournalTrends in Biochemical Sciences
Volume34
Issue number5
DOIs
Publication statusPublished - May 2009

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