Crystallization of the MS2 translational repressor alone and complexed to bromouridine
| Autor: | Bradley S. Hettinga, Phil Talbot, Michael M. Williamson, Reha Celikel, Craig Thulin, Roger Fourme, Richard S. Mitchell, Karen J. Krapcho, Kathryn R. Ely, John Wickersham, Raymond F. Gesteland, Chao-Zhou Ni, Thierry Prangé |
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| Jazyk: | angličtina |
| Rok vydání: | 1995 |
| Předmět: |
Protein Conformation
Dimer Mutant Repressor RNA RNA-Binding Proteins RNA-binding protein Biology Crystallography X-Ray Biochemistry Repressor Proteins Crystallography chemistry.chemical_compound Protein structure Capsid chemistry Bromodeoxyuridine Molecule Point Mutation Capsid Proteins Crystallization Molecular Biology Research Article Levivirus |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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