CRYSTALLIZATION OF THE MS2 TRANSLATIONAL REPRESSOR ALONE AND COMPLEXED TO BROMOURIDINE

Citation
Cz. Ni et al., CRYSTALLIZATION OF THE MS2 TRANSLATIONAL REPRESSOR ALONE AND COMPLEXED TO BROMOURIDINE, Protein science, 4(5), 1995, pp. 1010-1012
Citations number
15
Categorie Soggetti
Biology
Journal title
ISSN journal
09618368
Volume
4
Issue
5
Year of publication
1995
Pages
1010 - 1012
Database
ISI
SICI code
0961-8368(1995)4:5<1010:COTMTR>2.0.ZU;2-5
Abstract
The coat protein from the MS2 bacteriophage plays a dual role by encap sidating viral RNA and also by binding RNA as a translational represso r. In order to study the isolated dimer in a conformation not influenc ed by capsid interactions, a mutant molecule was crystallized that is defective in capsid assembly but is an active repressor. The unassembl ed dimer crystallized in the space group P2(1)2(1)2 with a = 76.2, b = 55.7, and c = 28.4 Angstrom. In these crystals, monomers were related by twofold symmetry. When this dimer was co-crystallized with 5-bromo uridine, crystals formed in space group R3 with a = b = 155.9 Angstrom , c = 29.9 Angstrom, gamma = 120 degrees; the dimer was the asymmetric unit.