Pro-Gly mediated conformational switch of mycobacteriophage D29 holin transmembrane domain I is lipid concentration driven

Chem Commun (Camb). 2013 Oct 25;49(83):9594-6. doi: 10.1039/c3cc45058a.

Abstract

Biophysical and spectroscopic analysis of synthetic transmembrane domain I (1) of mycobacteriophage D29 holin shows a lipid concentration dependent conformational switch from an α-helix to a β-sheet structure. The reversibility of this switch, upon change in the lipid-to-peptide ratio, requires a central Pro-Gly segment, and is abolished upon mutation to Ala-Ala or (D)Pro-Gly.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Dipeptides / chemistry*
  • Dipeptides / genetics
  • Dipeptides / metabolism
  • Hot Temperature
  • Lipid Metabolism
  • Molecular Sequence Data
  • Mycobacteriophages / chemistry
  • Mycobacteriophages / genetics
  • Mycobacteriophages / metabolism*
  • Mycobacterium tuberculosis / virology*
  • Protein Stability
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Viral Proteins / chemistry*
  • Viral Proteins / genetics
  • Viral Proteins / metabolism*

Substances

  • Dipeptides
  • Viral Proteins
  • prolylglycine