2c50 | pdb_00002c50

MS2-RNA HAIRPIN (A -5) COMPLEX

spinqualitylabelsall models 2c50, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2c50 is a 5 chain structure with sequence from Bacteriophage ms2. This structure supersedes the now removed PDB entry 1he6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1aq3, 1aq4, 1bms, 1dzs, 1gkv, 1gkw, 1h8j, 1kuo, 1msc, 1mst, 1mva, 1mvb, 1u1y, 1zdh, 1zdi, 1zdj, 1zdk, 2bny, 2bq5, 2bs0, 2bs1, 2bu1, 2c4z, 2c4y, 2c51, 2ms2, 5msf, 6msf, 7msf Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [COAT_BPMS2] Forms the phage shell; binds to the phage RNA. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural basis of pyrimidine specificity in the MS2 RNA hairpin-coat-protein complex.,Grahn E, Moss T, Helgstrand C, Fridborg K, Sundaram M, Tars K, Lago H, Stonehouse NJ, Davis DR, Stockley PG, Liljas L RNA. 2001 Nov;7(11):1616-27. PMID:11720290 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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