1AQ3

BACTERIOPHAGE MS2 CAPSID PROTEIN/RNA COMPLEX

Summary for 1AQ3

• Entry DOI: 10.2210/pdb1aq3/pdb
• Descriptor: RNA (5'-R(*AP*CP*AP*UP*GP*AP*GP*GP*AP*UP*UP*AP*CP*CP*CP*AP*U P*GP*U)-3'), PROTEIN (BACTERIOPHAGE MS2 COAT PROTEIN) (3 entities in total)
• Functional Keywords: complex (coat protein-rna), coat protein, rna-binding, viral protein capsid, rna fragment, icosahedral virus, virus-rna complex, virus/rna
• Biological source: Enterobacterio phage MS2
• Total number of polymer chains: 5
• Total formula weight: 53298.63

Authors

Van Den Worm, S.,Stonehouse, N.,Valegard, K.,Liljas, L. (deposition date: 1997-08-06, release date: 1997-12-24, Last modification date: 2024-04-03)

Primary citation

van den Worm, S.H.,Stonehouse, N.J.,Valegard, K.,Murray, J.B.,Walton, C.,Fridborg, K.,Stockley, P.G.,Liljas, L.
Crystal structures of MS2 coat protein mutants in complex with wild-type RNA operator fragments.
Nucleic Acids Res., 26:1345-1351, 1998

PubMed Abstract: In MS2 assembly of phage particles results from an interaction between a coat protein dimer and a stem-loop of the RNA genome (the operator hairpin). Amino acid residues Thr45, which is universally conserved among the small RNA phages, and Thr59 are part of the specific RNA binding pocket and interact directly with the RNA; the former through a hydrogen bond, the latter through hydrophobic contacts. The crystal structures of MS2 protein capsids formed by mutants Thr45Ala and Thr59Ser, both with and without the 19 nt wild-type operator hairpin bound, are reported here. The RNA hairpin binds to these mutants in a similar way to its binding to wild-type protein. In a companion paper both mutants are shown to be deficient in RNA binding in an in vivo assay, but in vitro the equilibrium dissociation constant is significantly higher than wild-type for the Thr45Ala mutant. The change in binding affinity of the Thr45Ala mutant is probably a direct consequence of removal of direct hydrogen bonds between the protein and the RNA. The properties of the Thr59Ser mutant are more difficult to explain, but are consistent with a loss of non-polar contact.

PubMed: 9469847
DOI: 10.1093/nar/26.5.1345

Experimental method

X-RAY DIFFRACTION (2.8 Å)