1ZSE
RNA stemloop from bacteriophage Qbeta complexed with an N87S mutant MS2 Capsid
Summary for 1ZSE
Entry DOI | 10.2210/pdb1zse/pdb |
Related | 1AQ3 1AQ4 1BMS 1DZS 1E6T 2BNY |
Descriptor | RNA HAIRPIN, Coat protein (3 entities in total) |
Functional Keywords | capsid, complex (capsid protein - rna hairpin), hairpin, levivirus, virus/viral protein/rna, rna-virus-viral protein complex, rna/virus/viral protein |
Biological source | Enterobacterio phage MS2 More |
Cellular location | Virion (Potential): P03612 |
Total number of polymer chains | 4 |
Total formula weight | 47526.18 |
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: 2005-05-24, release date: 2006-05-09, Last modification date: 2023-08-23) |
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, 14:487-495, 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 (3 Å) |
Structure validation
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