title: Pro-Gly mediated conformational switch of mycobacteriophage D29 holin transmembrane domain I is lipid concentration driven.
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.
authors.affiliation: Molecular Biophysics Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal, India. maha@iiserb.ac.in.
authors.forename: Muralikrishna
authors.initials: M
authors.lastname: Lella
authors.forename: Radhakrishnan
authors.initials: R
authors.lastname: Mahalakshmi
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D004151:Dipeptides / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006358:Hot Temperature; D050356:Lipid Metabolism; D008969:Molecular Sequence Data; D009160:Mycobacteriophages / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D009169:Mycobacterium tuberculosis / Q000821:virology*; D055550:Protein Stability; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D004151:Dipeptides; D014764:Viral Proteins; C057749:prolylglycine