Skip to main navigation Skip to search Skip to main content

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

    17 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

    Fingerprint

    Dive into the research topics of 'From 'I' to 'L' and back again: the odyssey of membrane-bound M13 protein'. Together they form a unique fingerprint.

    Cite this