Crystallization of the MS2 translational repressor alone and complexed to bromouridine.
Protein Sci
; 4(5): 1010-2, 1995 May.
Article
in En
| MEDLINE
| ID: mdl-7663336
ABSTRACT
The coat protein from the MS2 bacteriophage plays a dual role by encapsidating viral RNA and also by binding RNA as a translational repressor. In order to study the isolated dimer in a conformation not influenced by capsid interactions, a mutant molecule was crystallized that is defective in capsid assembly but is an active repressor. The unassembled dimer crystallized in the space group P21212 with a = 76.2, b = 55.7, and c = 28.4 A. In these crystals, monomers were related by twofold symmetry. When this dimer was co-crystallized with 5-bromouridine, crystals formed in space group R3 with a = b = 155.9 A, c = 29.9 A, gamma = 120 degrees; the dimer was the asymmetric unit.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bromodeoxyuridine
/
Capsid
/
RNA-Binding Proteins
/
Levivirus
/
Capsid Proteins
Language:
En
Journal:
Protein Sci
Journal subject:
BIOQUIMICA
Year:
1995
Document type:
Article
Affiliation country:
United States