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