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

Trends Biochem Sci. 2009 May;34(5):249-55. doi: 10.1016/j.tibs.2009.01.007. Epub 2009 Apr 8.

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.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacteriophage M13 / metabolism*
  • Capsid Proteins / chemistry*
  • Capsid Proteins / metabolism*
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism*
  • Models, Biological
  • Molecular Sequence Data
  • Protein Conformation

Substances

  • Capsid Proteins
  • Membrane Proteins