Crystallization of the MS2 translational repressor alone and complexed to bromouridine.
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.
Ni
C Z
CZ
Cancer Research Center, La Jolla Cancer Research Foundation, California 92037, USA.
Hettinga
B S
BS
Wickersham
J
J
Mitchell
R S
RS
Williamson
M M
MM
Celikel
R
R
Prangé
T
T
Fourme
R
R
Krapcho
K J
KJ
Thulin
C
C
D001973:Bromodeoxyuridine / Q000378:metabolism*; D002213:Capsid / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D036022:Capsid Proteins; D003460:Crystallization; D018360:Crystallography, X-Ray; D017909:Levivirus / Q000737:chemistry* / Q000235:genetics; D017354:Point Mutation; D011487:Protein Conformation; D016601:RNA-Binding Proteins; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D036022:Capsid Proteins; D016601:RNA-Binding Proteins; D012097:Repressor Proteins; D001973:Bromodeoxyuridine