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From 'I' to 'L' and back again: the odyssey of membrane-bound M13 protein.
Vos, Werner L; Nazarov, Petr V; Koehorst, Rob B M; Spruijt, Ruud B; Hemminga, Marcus A.
Affiliation
  • Vos WL; Department of Biology, National University of Ireland Maynooth, County Kildare, Ireland.
Trends Biochem Sci ; 34(5): 249-55, 2009 May.
Article in En | MEDLINE | ID: mdl-19362002
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.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacteriophage M13 / Capsid Proteins / Membrane Proteins Language: En Journal: Trends Biochem Sci Year: 2009 Document type: Article Affiliation country: Ireland

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacteriophage M13 / Capsid Proteins / Membrane Proteins Language: En Journal: Trends Biochem Sci Year: 2009 Document type: Article Affiliation country: Ireland