Crystal structures of a series of RNA aptamers complexed to the same protein target.
We have determined the crystal structures, at 2.8 A resolution, of two different RNA aptamers, each bound to MS2 coat protein. One of the aptamers contains a non-Watson-Crick base pair, while the other is missing one of the unpaired adenines that make sequence-specific contacts in the wild-type complex. Despite these differences, the RNA aptamers bind in the same location on the protein as the wild-type translational operator. Comparison of these new structures with other MS2-RNA complexes allows us to refine further the definition of the minimal recognition elements and suggests a possible application of the MS2 system for routine structure determination of small nucleic acid motifs.
Rowsell
S
S
School of Biochemistry and Molecular Biology, and North of England Structural Biology Centre, University of Leeds, UK.
Stonehouse
N J
NJ
Convery
M A
MA
Adams
C J
CJ
Ellington
A D
AD
Hirao
I
I
Peabody
D S
DS
Stockley
P G
PG
Phillips
S E
SE
D020029:Base Pairing; D002213:Capsid / Q000737:chemistry*; D036022:Capsid Proteins; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D012313:RNA / Q000737:chemistry*; D016601:RNA-Binding Proteins / Q000737:chemistry*
D036022:Capsid Proteins; D016601:RNA-Binding Proteins; D012313:RNA