2C4Z

MS2-RNA HAIRPIN (2SU -5-6) COMPLEX

Replaces:  1HDW

Summary for 2C4Z

• Entry DOI: 10.2210/pdb2c4z/pdb
• Related: 1AQ3 1AQ4 1BMS 1DZS 1GKV 1GKW 1H8J 1HE6 1KUO 1MSC 1MST 1MVA 1MVB 1U1Y 1ZDH 1ZDI 1ZDJ 1ZDK 2BNY 2BQ5 2BS0 2BS1 2BU1 2C4Y 2C50 2C51 2MS2 5MSF 6MSF 7MSF
• Descriptor: COAT PROTEIN, 5'-R(*AP*CP*AP*UP*GP*AP*GP*GP*AP*SUR *SUR*AP*CP*CP*CP*AP*UP*GP*U)-3' (3 entities in total)
• Functional Keywords: virus/rna, capsid, complex (capsid protein-rna hairpin), hairpin, levivirus, virus/viral protein/rna, virus coat protein, rna- binding, icosahedral virus, virus-rna complex
• Biological source: ENTEROBACTERIO PHAGE MS2; More
• Total number of polymer chains: 5
• Total formula weight: 53404.97

Authors

Grahn, E.,Moss, T.,Helgstrand, C.,Fridborg, K.,Sundaram, M.,Tars, K.,Lago, H.,Stonehouse, N.J.,Davis, D.R.,Stockley, P.G.,Liljas, L. (deposition date: 2005-10-25, release date: 2006-01-05, Last modification date: 2023-12-13)

Primary citation

Grahn, E.,Moss, T.,Helgstrand, C.,Fridborg, K.,Sundaram, M.,Tars, K.,Lago, H.,Stonehouse, N.J.,Davis, D.R.,Stockley, P.G.,Liljas, L.
Structural basis of pyrimidine specificity in the MS2 RNA hairpin-coat-protein complex.
Rna, 7:1616-1627, 2001

PubMed Abstract: We have determined the X-ray structures of six MS2 RNA hairpin-coat-protein complexes having five different substitutions at the hairpin loop base -5. This is a uracil in the wild-type hairpin and contacts the coat protein both by stacking on to a tyrosine side chain and by hydrogen bonding to an asparagine side chain. The RNA consensus sequence derived from coat protein binding studies with natural sequence variants suggested that the -5 base needs to be a pyrimidine for strong binding. The five -5 substituents used in this study were 5-bromouracil, pyrimidin-2-one, 2-thiouracil, adenine, and guanine. The structure of the 5-bromouracil complex was determined to 2.2 A resolution, which is the highest to date for any MS2 RNA-protein complex. All the complexes presented here show very similar conformations, despite variation in affinity in solution. The results suggest that the stacking of the -5 base on to the tyrosine side chain is the most important driving force for complex formation. A number of hydrogen bonds that are present in the wild-type complex are not crucial for binding, as they are missing in one or more of the complexes. The results also reveal the flexibility of this RNA-protein interface, with respect to functional group variation, and may be generally applicable to other RNA-protein complexes.

PubMed: 11720290

Experimental method

X-RAY DIFFRACTION (2.6 Å)