Crystal structure of the MS2 coat protein dimer: implications for RNA binding and virus assembly

Ni, Chao-Zhou; Syed, Rashid; Kodandapani, R.; Wickersham, John; Peabody, David S.; Ely, Kathryn R.

doi:10.1016/s0969-2126(01)00156-3

Cited by 89 publications

(98 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In our previous studies, we crystallized the MS2 coat protein in the dimer form rather than as capsids (Ni et al, 1995). This was made possible by the existence of mutants defective for the assembly of capsids (Peabody & Ely, 1992).…”

Section: Resultsmentioning

confidence: 99%

“…The crystal structures of two intact Group I viruses (MS2: Valeg5rd et al, 1990;Golmohammadi et al, 1993;fr: Liljas et al, 1994) and one Group 111 virus (QP: Golmohammadi et al, 1996) have been determined, and we described the structure of the MS2 unassembled coat protein dimer previously (Ni et al, 1995). How-2485 ever, no crystal structure has yet been reported for a Group I1 bacteriophage.…”

mentioning

confidence: 97%

“…We had reported previously the crystal structure of the unassembled MS2 dimer (Ni et al, 1995) and compared this structure to the coat protein in the viral capsid (Golmohammadi et al, 1993). In this report, we directly compare the structures of the GA and MS2 unassembled dimers.…”

mentioning

confidence: 99%

“…Sequence differences between these coat proteins that may affect tertiary folding or capsid formation are also highlighted. Critical sites for virus assembly identified from our comparison of the MS2 dimer with the MS2 capsid (Ni et al, 1995) are located on the GA model.…”

mentioning

confidence: 99%

“…The RNA contact residues in GA are compared to corresponding residues in the MS2 virus-operator complex and to these same residues in the unliganded MS2 dimer (Ni et al, 1995). Direct comparisons of the RNA-binding sites of the GA and MS2 repressors in the unassembled dimers represent molecular conformations that are not influenced by capsid interactions.…”

mentioning

confidence: 99%

See 4 more Smart Citations

Crystal structure of the coat protein from the GA bacteriophage: Model of the unassembled dimer

White

Mitchell

et al. 1996

Protein Science

Self Cite

View full text Add to dashboard Cite

There are four groups of RNA bacteriophages with distinct antigenic and physicochemical properties due to differences in surface residues of the viral coat proteins. Coat proteins also play a role as translational repressor during the viral life cycle, binding an RNA hairpin within the genome. In this study, the first crystal structure of the coat protein from a Group I1 phage GA is reported and compared to the Group I MS2 coat protein. The structure of the GA dimer was determined at 2.8 8, resolution (R-factor = 0.20). The overall folding pattern of the coat protein is similar to the Group I MS2 coat protein in the intact virus (Golmohammadi R, Valegird K, Fridborg K, Liljas L, 1993, J Mol Biol234:620-639) or as an unassembled dimer (Ni CZ, Syed R, Kodandapani R, Wickersham J, Peabody DS, Ely KR, 1995, Srructure 3:255-263). The structures differ in the FG loops and in the first turn of the a A helix. GA and MS2 coat proteins differ in sequence at 49 of 129 amino acid residues. Sequence differences that contribute to distinct immunological and physical properties of the proteins are found at the surface of the intact virus in the AB and FG loops. There are six differences in potential RNA contact residues within the RNA-binding site located in an antiparallel @sheet across the dimer interface. Three differences involve residues in the center of this concave site: Lys/Arg 83, Ser/Asn 87, and Asp/Glu 89. Residue 87 was shown by molecular genetics to define RNA-binding specificity by GA or MS2 coat protein (Lim F, Spingola M, Peabody DS, 1994, J BioZ Chem 269:9006-9010). This sequence difference reflects recognition of the nucleotide at position -5 in the unpaired loop of the translational operators bound by these coat proteins. In GA, the nucleotide at this position is a purine whereas in MS2, it is a pyrimidine.Keywords: bacteriophage coat protein; crystal structure; RNA hairpin; translational repressor; virus RNA bacteriophages are small viruses with a simple organization. These viruses have an icosahedral shell composed of 180 copies of coat protein and one copy of the maturation protein that encapsidate genomic RNA ,which is approximately 3,500 nucleotides in length. The single-stranded RNA genome also acts as mRNA, encoding four proteins: the viral coat protein, a maturation protein, a replicase subunit, and the lysis protein. These phages were first isolated from Escherichia coli, but later were also found in Caulobacter and Pseudomonas. To date, the coliphages have been the best studied and are classified into four groups based on serological and physicochemical properties. Groups I and I1 are quite similar, with MS2 and GA phages being the well-characterized members of these groups. Phages Q p and SP, members of Groups I11 and IV, respectively, are more divergent from Groups I and 11.

show abstract

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 97%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Crystal structure of the coat protein from the GA bacteriophage: Model of the unassembled dimer

White

Mitchell

et al. 1996

Protein Science

Self Cite

View full text Add to dashboard Cite

show abstract

SyntheticRNAScaffolds for Spatial Engineering in Cells

Sachdeva

Myhrvold

Yin³

2018

Synthetic Biology

View full text Add to dashboard Cite

Mutagenesis of a stacking contact in the MS2 coat protein-RNA complex.

1996

View full text Add to dashboard Cite

The thermodynamic contribution of a stacking interaction between Tyr85 in MS2 coat protein and a single‐stranded pyrimidine in its RNA binding site has been examined. Mutation of Tyr85 to Phe, His, Cys, Ser and Ala decreased the RNA affinity by 1–3 kcal/mol under standard binding conditions. Since the Phe, His and Cys 85 proteins formed UV photocrosslinks with iodouracil‐containing RNA at the same rate as the wild‐type protein, the mutant proteins interact with RNA in a similar manner. The pH dependence of KD for the Phe and His proteins differs substantially from the wild‐type protein, suggesting that the titration of position 85 contributes substantially to the binding properties. Experiments with specifically substituted phosphorothioate RNAs confirm a hydrogen bond between the hydroxyl group of tyrosine and a phosphate predicted by the crystal structure.

show abstract

Crystal structure of the MS2 coat protein dimer: implications for RNA binding and virus assembly

Cited by 89 publications

References 23 publications

Crystal structure of the coat protein from the GA bacteriophage: Model of the unassembled dimer

Crystal structure of the coat protein from the GA bacteriophage: Model of the unassembled dimer

SyntheticRNAScaffolds for Spatial Engineering in Cells

Mutagenesis of a stacking contact in the MS2 coat protein-RNA complex.

Contact Info

Product

Resources

About