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Crystallization of the MS2 translational repressor alone and complexed to bromouridine
Author(s) -
Ni ChaoZhou,
Hettinga Bradley S.,
Wickersham John,
Mitchell Richard S.,
Williamson Michael M.,
Celikel Reha,
Ely Kathryn R.,
Prangé Thierry,
Fourme Roger,
Krapcho Karen J.,
Thulin Craig,
Talbot Phil,
Gesteland Raymond F.
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560040522
Subject(s) - dimer , capsid , repressor , monomer , rna , chemistry , crystallization , bacteriophage ms2 , mutant , crystallography , biophysics , biology , biochemistry , coat protein , gene , transcription factor , organic chemistry , polymer
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 P2 1 2 1 2 with a = 76.2, b = 55.7, and c = 28.4 Å. In these crystals, monomers were related by twofold symmetry. When this dimer was co‐crystallized with 5‐bromouridine, crystals formed in space group R 3 with a = b = 155.9 Å, c = 29.9 Å, γ = 120°; the dimer was the asymmetric unit.