2BS1
MS2 (N87AE89K mutant) - Qbeta RNA hairpin complex
Summary for 2BS1
Entry DOI | 10.2210/pdb2bs1/pdb |
Related | 1AQ3 1AQ4 1BMS 1DZS 1GKV 1GKW 1KUO 1MSC 1MST 1MVA 1MVB 1U1Y 1ZDH 1ZDI 1ZDJ 1ZDK 2BNY 2BQ5 2BS0 2BU1 2C4Q 2C4Y 2C4Z 2C50 2C51 2MS2 5MSF 6MSF 7MSF |
Descriptor | MS2 COAT PROTEIN, 5'-R(*AP*CP*AP*UP*GP*AP*GP*GP*AP*UP *UP*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, icosahedral virus, virus-rna complex |
Biological source | BACTERIOPHAGE MS2 More |
Cellular location | Virion (Potential): P03612 |
Total number of polymer chains | 5 |
Total formula weight | 53870.24 |
Authors | Horn, W.T.,Tars, K.,Grahn, E.,Helgstrand, C.,Baron, A.J.,Lago, H.,Adams, C.J.,Peabody, D.S.,Phillips, S.E.V.,Stonehouse, N.J.,Liljas, L.,Stockley, P.G. (deposition date: 2005-05-13, release date: 2006-03-22, Last modification date: 2023-12-13) |
Primary citation | Horn, W.T.,Tars, K.,Grahn, E.,Helgstrand, C.,Baron, A.J.,Lago, H.,Adams, C.J.,Peabody, D.S.,Phillips, S.E.V.,Stonehouse, N.J.,Liljas, L.,Stockley, P.G. Structural Basis of RNA Binding Discrimination between Bacteriophages Qbeta and MS2. Structure, 14:487-, 2006 Cited by PubMed Abstract: Sequence-specific interactions between RNA stem-loops and coat protein (CP) subunits play vital roles in the life cycles of the RNA bacteriophages, e.g., by allowing translational repression of their replicase cistrons and tagging their own RNA genomes for encapsidation. The CPs of bacteriophages Qbeta and MS2 each discriminate in favor of their cognate translational operators, even in the presence of closely related operators from other phages in vivo. Discrete mutations within the MS2 CP have been shown to relax this discrimination in vitro. We have determined the structures of eight complexes between such mutants and both MS2 and Qbeta stem-loops with X-ray crystallography. In conjunction with previously determined in vivo repression data, the structures enable us to propose the molecular basis for the discrimination mechanism. PubMed: 16531233DOI: 10.1016/J.STR.2005.12.006 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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